Spectrum analysis Books

Book SynopsisPresents basic concepts, experimental methodology and data acquisition, and processing standards of in vivo NMR spectroscopy This book covers, in detail, the technical and biophysical aspects of in vivo NMR techniques and includes novel developments in the field such as hyperpolarized NMR, dynamic 13C NMR, automated shimming, and parallel acquisitions. Most of the techniques are described from an educational point of view, yet it still retains the practical aspects appreciated by experimental NMR spectroscopists. In addition, each chapter concludes with a number of exercises designed to review, and often extend, the presented NMR principles and techniques. The third edition of In Vivo NMR Spectroscopy: Principles and Techniques has been updated to include experimental detail on the developing area of hyperpolarization; a description of the semi-LASER sequence, which is now a method of choice; updated chemical shift data, includingTable of ContentsPreface xv Abbreviations xvii Supplementary Material xxiv 1 Basic Principles 1 1.1 Introduction 1 1.2 Classical Magnetic Moments 3 1.3 Nuclear Magnetization 5 1.4 Nuclear Induction 9 1.5 Rotating Frame of Reference 11 1.6 Transverse T2 and T2 * Relaxation 12 1.7 Bloch Equations 16 1.8 Fourier Transform NMR 17 1.9 Chemical Shift 20 1.10 Digital NMR 23 1.10.1 Analog‐to‐digital Conversion 23 1.10.2 Signal Averaging 25 1.10.3 Digital Fourier Transformation 25 1.10.4 Zero Filling 25 1.10.5 Apodization 26 1.11 Quantum Description of NMR 28 1.12 Scalar Coupling 30 1.13 Chemical and Magnetic Equivalence 33 Exercises 37 References 40 2 In Vivo NMR Spectroscopy – Static Aspects 43 2.1 Introduction 43 2.2 Proton NMR Spectroscopy 43 2.2.1 Acetate (Ace) 51 2.2.2 N‐Acetyl Aspartate (NAA) 52 2.2.3 N‐Acetyl Aspartyl Glutamate (NAAG) 53 2.2.4 Adenosine Triphosphate (ATP) 54 2.2.5 Alanine (Ala) 55 2.2.6 γ‐Aminobutyric Acid (GABA) 56 2.2.7 Ascorbic Acid (Asc) 57 2.2.8 Aspartic Acid (Asp) 58 2.2.9 Branched‐chain Amino Acids (Isoleucine, Leucine, and Valine) 58 2.2.10 Choline‐containing Compounds (tCho) 59 2.2.11 Creatine (Cr) and Phosphocreatine (PCr) 61 2.2.12 Ethanol 62 2.2.13 Ethanolamine (EA) and Phosphorylethanolamine (PE) 63 2.2.14 Glucose (Glc) 63 2.2.15 Glutamate (Glu) 64 2.2.16 Glutamine (Gln) 65 2.2.17 Glutathione (GSH) 66 2.2.18 Glycerol 67 2.2.19 Glycine 68 2.2.20 Glycogen 68 2.2.21 Histidine 69 2.2.22 Homocarnosine 70 2.2.23 β‐Hydoxybutyrate (BHB) 70 2.2.24 2‐Hydroxyglutarate (2HG) 71 2.2.25 myo‐Inositol (mI) and scyllo‐Inositol (sI) 72 2.2.26 Lactate (Lac) 73 2.2.27 Macromolecules 74 2.2.28 Nicotinamide Adenine Dinucleotide (NAD+) 76 2.2.29 Phenylalanine 76 2.2.30 Pyruvate 77 2.2.31 Serine 78 2.2.32 Succinate 79 2.2.33 Taurine (Tau) 79 2.2.34 Threonine (Thr) 80 2.2.35 Tryptophan (Trp) 80 2.2.36 Tyrosine (Tyr) 80 2.2.37 Water 81 2.2.38 Non‐cerebral Metabolites 82 2.2.39 Carnitine and Acetyl‐carnitine 82 2.2.40 Carnosine 84 2.2.41 Citric Acid 86 2.2.42 Deoxymyoglobin (DMb) 87 2.2.43 Lipids 87 2.2.44 Spermine and Polyamines 89 2.3 Phosphorus‐31 NMR Spectroscopy 90 2.3.1 Chemical Shifts 90 2.3.2 Intracellular pH 92 2.4 Carbon‐13 NMR Spectroscopy 93 2.4.1 Chemical Shifts 93 2.5 Sodium‐23 NMR Spectroscopy 96 2.6 Fluorine‐19 NMR Spectroscopy 102 2.7 In vivo NMR on Other Non‐proton Nuclei 104 Exercises 106 References 108 3 In Vivo NMR Spectroscopy – Dynamic Aspects 129 3.1 Introduction 129 3.2 Relaxation 129 3.2.1 General Principles of Dipolar Relaxation 129 3.2.2 Nuclear Overhauser Effect 133 3.2.3 Alternative Relaxation Mechanisms 134 3.2.4 Effects of T1 Relaxation 137 3.2.5 Effects of T2 Relaxation 138 3.2.6 Measurement of T1 and T2 Relaxation 141 3.2.6.1 T1 Relaxation 141 3.2.6.2 Inversion Recovery 141 3.2.6.3 Saturation Recovery 142 3.2.6.4 Variable Nutation Angle 142 3.2.6.5 MR Fingerprinting 143 3.2.6.6 T2 Relaxation 143 3.2.7 In Vivo Relaxation 144 3.3 Magnetization Transfer 147 3.3.1 Principles of MT 149 3.3.2 MT Methods 150 3.3.3 Multiple Exchange Reactions 152 3.3.4 MT Contrast 152 3.3.5 Chemical Exchange Saturation Transfer (CEST) 156 3.4 Diffusion 160 3.4.1 Principles of Diffusion 160 3.4.2 Diffusion and NMR 160 3.4.3 Anisotropic Diffusion 169 3.4.4 Restricted Diffusion 173 3.5 Dynamic NMR of Isotopically‐Enriched Substrates 175 3.5.1 General Principles and Setup 177 3.5.2 Metabolic Modeling 177 3.5.3 Thermally Polarized Dynamic 13C NMR Spectroscopy 184 3.5.3.1 [1‐13C]‐Glucose and [1,6‐13C2]‐Glucose 184 3.5.3.2 [2‐13C]‐Glucose 185 3.5.3.3 [U‐13C6]‐Glucose 187 3.5.3.4 [2‐13C]‐Acetate 187 3.5.4 Hyperpolarized Dynamic 13C NMR Spectroscopy 189 3.5.4.1 Brute Force Hyperpolarization 189 3.5.4.2 Optical Pumping of Noble Gases 190 3.5.4.3 Parahydrogen‐induced Polarization (PHIP) 191 3.5.4.4 Signal Amplification by Reversible Exchange (SABRE) 193 3.5.4.5 Dynamic Nuclear Polarization (DNP) 193 3.5.5 Deuterium Metabolic Imaging (DMI) 196 Exercises 197 References199 4 Magnetic Resonance Imaging 211 4.1 Introduction 211 4.2 Magnetic Field Gradients 211 4.3 Slice Selection 212 4.4 Frequency Encoding 215 4.4.1 Principle 215 4.4.2 Echo Formation 216 4.5 Phase Encoding 219 4.6 Spatial Frequency Space 221 4.7 Fast MRI Sequences 225 4.7.1 Reduced TR Methods 225 4.7.2 Rapid k‐Space Traversal 226 4.7.3 Parallel MRI 229 4.7.3.1 SENSE 230 4.7.3.2 GRAPPA 233 4.8 Contrast in MRI 234 4.8.1 T1 and T2 Relaxation Mapping 236 4.8.2 Magnetic Field B0 Mapping 239 4.8.3 Magnetic Field B1 Mapping 241 4.8.4 Alternative Image Contrast Mechanisms 242 4.8.5 Functional MRI 243 Exercises 245 References 249 5 Radiofrequency Pulses 253 5.1 Introduction 253 5.2 Square RF Pulses 253 5.3 Selective RF Pulses 259 5.3.1 Fourier‐transform‐based RF Pulses 260 5.3.2 RF Pulse Characteristics 262 5.3.3 Optimized RF Pulses 266 5.3.4 Multifrequency RF Pulses 269 5.4 Composite RF Pulses 271 5.5 Adiabatic RF Pulses 273 5.5.1 Rotating Frame of Reference 275 5.5.2 Adiabatic Condition 276 5.5.3 Modulation Functions 278 5.5.4 AFP Refocusing 280 5.5.5 Adiabatic Plane Rotation of Arbitrary Nutation Angle 282 5.6 Multidimensional RF Pulses 284 5.7 Spectral–Spatial RF Pulses 284 Exercises 286 References 288 6 Single Volume Localization and Water Suppression 293 6.1 Introduction 293 6.2 Single‐volume Localization 294 6.2.1 Image Selected In Vivo Spectroscopy (ISIS) 295 6.2.2 Chemical Shift Displacement 297 6.2.3 Coherence Selection 301 6.2.3.1 Phase Cycling 302 6.2.3.2 Magnetic Field Gradients 302 6.2.4 STimulated Echo Acquisition Mode (STEAM) 304 6.2.5 Point Resolved Spectroscopy (PRESS) 307 6.2.6 Signal Dephasing with Magnetic Field Gradients 309 6.2.7 Localization by Adiabatic Selective Refocusing (LASER) 314 6.3 Water Suppression 317 6.3.1 Binomial and Related Pulse Sequences 318 6.3.2 Frequency‐Selective Excitation 321 6.3.3 Frequency‐Selective Refocusing 323 6.3.4 Relaxation‐Based Methods 323 6.3.5 Non‐water‐suppressed NMR Spectroscopy 326 Exercises 327 References 330 7 Spectroscopic Imaging and Multivolume Localization 335 7.1 Introduction 335 7.2 Principles of MRSI 335 7.3 k‐Space Description of MRSI 338 7.4 Spatial Resolution in MRSI 339 7.5 Temporal Resolution in MRSI 341 7.5.1 Conventional Methods 343 7.5.1.1 Circular and Spherical k‐Space Sampling 343 7.5.1.2 k‐Space Apodization During Acquisition 343 7.5.1.3 Zoom MRSI 345 7.5.2 Methods Based on Fast MRI 346 7.5.2.1 Echo‐planar Spectroscopic Imaging (EPSI) 346 7.5.2.2 Spiral MRSI 349 7.5.2.3 Parallel MRSI 350 7.5.3 Methods Based on Prior Knowledge 351 7.6 Lipid Suppression 353 7.6.1 Relaxation‐based Methods 353 7.6.2 Inner Volume Selection and Volume Prelocalization 355 7.6.3 Outer Volume Suppression (OVS) 357 7.7 MR Spectroscopic Image Processing and Display 360 7.8 Multivolume Localization 364 7.8.1 Hadamard Localization 365 7.8.2 Sequential Multivolume Localization 366 Exercises 368 References370 8 Spectral Editing and 2D NMR 375 8.1 Introduction 375 8.2 Quantitative Descriptions of NMR 375 8.2.1 Density Matrix Formalism 376 8.2.2 Classical Vector Model 377 8.2.3 Correlated Vector Model 378 8.2.4 Product Operator Formalism 379 8.3 Scalar Evolution 380 8.4 J‐Difference Editing 384 8.4.1 Principle 384 8.4.2 Practical Considerations 385 8.4.3 GABA, 2HG, and Lactate 389 8.5 Multiple Quantum Coherence Editing 395 8.6 Spectral Editing Alternatives 400 8.7 Heteronuclear Spectral Editing 402 8.7.1 Proton‐observed, Carbon‐edited (POCE) MRS 402 8.7.2 Polarization Transfer – INEPT and DEPT 407 8.8 Broadband Decoupling 410 8.9 Sensitivity 414 8.10 Two‐dimensional NMR Spectroscopy 415 8.10.1 Correlation Spectroscopy (COSY) 416 8.10.2 J‐resolved Spectroscopy (JRES) 422 8.10.3 In vivo 2D NMR Methods 424 Exercises 429 References 432 9 Spectral Quantification 439 9.1 Introduction 439 9.2 Data Acquisition 440 9.2.1 Magnetic Field Homogeneity 440 9.2.2 Spatial Localization 442 9.2.3 Water Suppression 442 9.2.4 Sensitivity 442 9.3 Data Preprocessing 443 9.3.1 Phased‐array Coil Combination 443 9.3.2 Phasing and Frequency Alignment 444 9.3.3 Line‐shape Correction 444 9.3.4 Removal of Residual Water 444 9.3.5 Baseline Correction 446 9.4 Data Quantification 447 9.4.1 Time‐ and Frequency‐domain Parameters 447 9.4.2 Prior Knowledge 450 9.4.3 Spectral Fitting Algorithms 453 9.4.4 Error Estimation 457 9.5 Data Calibration 460 9.5.1 Partial Saturation 461 9.5.2 Nuclear Overhauser Effects 462 9.5.3 Transverse Relaxation 462 9.5.4 Diffusion 462 9.5.5 Scalar Coupling 462 9.5.6 Localization 463 9.5.7 Frequency‐dependent Amplitude‐ and Phase Distortions 463 9.5.8 NMR Visibility 463 9.5.9 Internal Concentration Reference 464 9.5.10 External Concentration Reference 466 9.5.11 Phantom Replacement Concentration Reference 466 Exercises 467 References 469 10 Hardware 473 10.1 Introduction 473 10.2 Magnets 473 10.3 Magnetic Field Homogeneity 478 10.3.1 Origins of Magnetic Field Inhomogeneity 478 10.3.2 Effects of Magnetic Field Inhomogeneity 482 10.3.3 Principles of Spherical Harmonic Shimming 485 10.3.4 Practical Spherical Harmonic Shimming 489 10.3.5 Alternative Shimming Strategies 491 10.4 Magnetic Field Gradients 493 10.4.1 Eddy Currents 498 10.4.2 Preemphasis 499 10.4.3 Active Shielding 503 10.5 Radiofrequency (RF) Coils 503 10.5.1 Electrical Circuit Analysis 503 10.5.2 RF Coil Performance 509 10.5.3 Spatial Field Properties 510 10.5.3.1 Longitudinal Magnetic Fields 512 10.5.3.2 Transverse Magnetic Fields 513 10.5.4 Principle of Reciprocity 514 10.5.4.1 Electromagnetic Wave Propagation 515 10.5.5 Parallel Transmission 517 10.5.6 RF Power and Specific Absorption Rate (SAR) 519 10.5.7 Specialized RF Coils 520 10.5.7.1 Combined Transmit and Receive RF Coils 521 10.5.7.2 Phased‐Array Coils 522 10.5.7.3 1H‐[13C] and 13C‐[1H] RF Coils 522 10.5.7.4 Cooled and Superconducting RF Coils 525 10.6 Complete MR System 526 10.6.1 RF Transmission 526 10.6.2 Signal Reception 527 10.6.3 Quadrature Detection 528 10.6.4 Dynamic Range 529 10.6.5 Gradient and Shim Systems 530 Exercises 531 References 534 Appendix A 541 A.1 Matrix Calculations 541 A.2 Trigonometric Equations 543 A.3 Fourier Transformation 543 A.3.1 Introduction 543 A.3.2 Properties 544 A.3.2.1 Linearity 544 A.3.2.2 Time and Frequency Shifting 544 A.3.2.3 Scaling 545 A.3.2.4 Convolution 545 A.3.3 Discrete Fourier Transformation 545 A.4 Product Operator Formalism 546 A.4.1 Cartesian Product Operators 546 A.4.2 Shift (Lowering and Raising) Operators 548 References 550 Further Reading 551 Index 553

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Book SynopsisIntroduces the reader to a wide range of spectroscopies and includes both the background theory and applications to structure determination and chemical analysis. It covers rotational, vibrational, electronic, photoelectron and Auger spectroscopy, as well as EXAFs and the theory of lasers and laser spectroscopy.Trade Review"Two valuable features for both students and instructors are a strong final chapter on Lasers and Laser Spectroscopy, and a set of 17 worked examples…" (Journal of Chemical Education, January 2005) "…a good reference for those interested in basic theories behind general spectroscopic techniques. I welcome its presence in my professional library." (Clinical Chemistry, December 2004) "…this text is well written and the descriptions relating theory to phenomena are clear and well constructed. The book achieves its goal as a well-rounded textbook." (Applied Spectroscopy, August 2004)Table of ContentsPreface to First Edition. Preface to Second Edition. Preface to Third Edition. Preface to Fourth Edition. Units, Dimensions and Conventions. Fundamental Constants. Useful Conversion Factors. 1. Some Important Results in Quantum Mechanics. 2. Electromagnetic Radiation and Its Interaction with Atoms and Molecules. 3. General Features of Experimental Methods. 4. Molecular Symmetry. 5. Rotational Spectroscopy. 6. Vibrational Spectroscopy. 7. Electronic Spectroscopy. 8. Photoelectron and Related Spectroscopies. 9. Lasers and Laser Spectroscopy. Appendix A: Character Tables. Appendix B: Symmetry Species of Vibrations. Index of Atoms and Molecules. Subject Index.

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Book SynopsisThe text Organic Structures from 2D NMR Spectra contains a graded set of structural problems employing 2D-NMR spectroscopy. The Instructors Guide and Solutions Manual to Organic Structures from 2D NMR Spectra is a set of step-by-step worked solutions to every problem in Organic Structures from 2D NMR Spectra. While it is absolutely clear that there are many ways to get to the correct solution of any of the problems, the instructors guide contains at least one complete pathway to every one of the questions. In addition, the instructors guide carefully rationalises every peak in every spectrum in relation to the correct structure. The Instructors Guide and Solutions Manual to Organic Structures from 2D NMR Spectra: Is a complete set of worked solutions to the problems contained in Organic Structures from 2D NMR Spectra. Provides a step-by-step description of the process to derive structures from spectra as well as annotated 2D spectra indicating the origin of every cross peak. HighlightsTable of ContentsPreface ix Solutions Summary 1 Problem 1 (1-iodopropane) 7 Problem 2 (2-butanone) 11 Problem 3 (2-hexanone) 15 Problem 4 (ethyl propionate) 19 Problem 5 (ethyl 3-ethoxypropionate) 23 Problem 6 (4-acetylbutyric acid) 28 Problem 7 (3-ethoxypropionyl chloride) 32 Problem 8 (ethyl 3-chloropropionate) 36 Problem 9 (isoamyl acetate) 40 Problem 10 (trans-4-hexen-3-one) 45 Problem 11 (trans-2-octen-4-one) 50 Problem 12 (3-nitrobenzaldehyde) 55 Problem 13 (3-iodotoluene) 61 Problem 14 (8-hydroxy-5-nitroquinoline) 64 Problem 15 (2-bromo-3-picoline) 69 Problem 16 (trans-anethole) 72 Problem 17 (cis-2-pentene) 75 Problem 18 (p-tolyl benzoate) 79 Problem 19 (phenyl p-toluate) 86 Problem 20 (4-biphenylyl acetate) 93 Problem 21 (4 ′ -phenoxyacetophenone) 99 Problem 22 (4 ′ -tert-butylacetophenone) 106 Problem 23 (2,2,4 ′ -trimethylpropiophenone) 110 Problem 24 (trans-2-methyl-3-phenyl-2-propen-1-ol) 114 Problem 25 (methyl 4-ethoxybenzoate) 119 Problem 26 (methyl 3-(p-tolyl)propionate) 123 Problem 27 (4-(4 ′ -methoxyphenyl)-2-butanone) 127 Problem 28 (ethyl 6-bromohexanoate) 132 Problem 29 (piperonal) 135 Problem 30 (cis-3-hexenyl benzoate) 139 Problem 31 (trans-2,cis-6-nonadienal) 146 Problem 32 (allyl glycidyl ether) 155 Problem 33 (3,4-epoxy-4-methyl-2-pentanone) 159 Problem 34 (dl-methionine) 162 Problem 35 (N-acetyl-l-leucine) 165 Problem 36 (isoamyl valerate) 170 Problem 37 ((E)-4-methyl-4 ′ -nitrostilbene) 173 Problem 38 (2-tert-butyl-6-methylphenol) 181 Problem 39 (2-allyl-6-methylphenol) 186 Problem 40 (2-hydroxy-4-methoxybenzaldehyde) 194 Problem 41 (2 ′ -hydroxy-5 ′ -methylacetophenone) 198 Problem 42 (3 ′ -fluoro-4 ′ -methoxyacetophenone) 203 Problem 43 (trans-ferulic acid) 209 Problem 44 (sec-butyl 3-hydroxycinnamate) 215 Problem 45 (1-benzosuberone) 221 Problem 46 (dimethyl (3-bromopropyl)phosphonate) 228 Problem 47 (caffeine) 233 Problem 48 (benzyloxypropionitrile) 238 Problem 49 (cineole) 242 Problem 50 (thymoquinone) 246 Problem 51 (4-bromo-1-indanol) 251 Problem 52 (1-bromo-4-methylnaphthalene) 257 Problem 53 (carvacrol) 264 Problem 54 (acetoacetanilide) 272 Problem 55 (ethyl acetamidocyanoacetate) 277 Problem 56 (α-humulene) 283 Problem 57 (3,4-dihydro-2H-benzopyran-3-carboxylic acid) 289 Problem 58 (quinidine) 296 Problem 59 (salbutamol) 312 Problem 60 (2-hydroxy-1-naphthaldehyde) 322 Problem 61 (6-methyl-4-chromanone) 329 Problem 62 (citronellal) 336 Problem 63 ((+)-cis-2-oxabicyclo-[3.3.0]oct-6-en-3-one) 344 Problem 64 (melatonin) 349 Problem 65 (carvone) 362 Problem 66 (haloperidol) 370

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Book Synopsisto Fluorescence.- Instrumentation for Fluorescence Spectroscopy.- Fluorophores.- Time-Domain Lifetime Measurements.- Frequency-Domain Lifetime Measurements.- Solvent and Environmental Effects.- Dynamics of Solvent and Spectral Relaxation.- Quenching of Fluorescence.- Mechanisms and Dynamics of Fluorescence Quenching.- Fluorescence Anisotropy.- Time-Dependent Anisotropy Decays.- Advanced Anisotropy Concepts.- Energy Transfer.- Time-Resolved Energy Transfer and Conformational Distributions of Biopolymers.- Energy Transfer to Multiple Acceptors in One,Two, or Three Dimensions.- Protein Fluorescence.- Time-Resolved Protein Fluorescence.- Multiphoton Excitation and Microscopy.- Fluorescence Sensing.- Novel Fluorophores.- DNA Technology.- Fluorescence-Lifetime Imaging Microscopy.- Single-Molecule Detection.- Fluorescence Correlation Spectroscopy.- Radiative Decay Engineering: Metal-Enhanced Fluorescence.- Radiative-Decay Engineering: Surface Plasmon-Coupled Emission.Trade ReviewPraise for Earlier Editions: "Lakowicz’s Principles of Fluorescence Spectroscopy has been the best one-volume introduction to the biophysical principles of fluorescence methods. - Roger Y. Tsien, Ph.D., Department of Pharmacology and Department of Chemistry and Biochemistry, University of California, San Diego, California "Principles of Fluorescence Spectroscopy is encyclopedic and comprehensive." - Britton Chance, Professor Emeritus in Biochemistry and Biophysics,University of Pennsylvania, School of Medicine, Philadelphia, Pennsylvania "Recommended without reservation both to the novice and to the expert in fluorescence." - Analytical Biochemistry "In addition to its use as a student text, it should be a particularly valuable reference for those involved in biochemical research." - Chemistry in Britain Advance Praise for Third Edition: "This third edition has significantly expanded the topics, and will remain as a leading reference, as well as a text…the information in the book is valuable for a wide range of disciplines." - Robert M. Clegg, Ph.D., Department of Physics, University of Illinois, Champaign-Urbana, Illinois "Overall this is a most welcome, and timely transformation of the classic, and most comprehensive textbook on fluorescence spectroscopy. It should be the number one item on the shopping list for any student or researcher involved in any aspect of fluorescence, be it as a biologist who does some microscopy, or a chemist synthesizing novel fluorophores." - Alan Ryder, Ph.D., National Centre for Biomedical Engineering Science, National University of Ireland-Galway, Galway, Ireland From the reviews of the third edition: "This book gives an overview of the principles and applications of fluorescence. It is well structured, starting with basic knowledge about the phenomena of fluorescence and ending with the latest applications. … highly readable and informative both by novices and by experienced people. … a helpful work of reference and a wonderful creation for learning and teaching. The updated 3rd edition with its appealing design and its absolutely up-to-date and, nevertheless, complete treatment of fluorescence spectroscopy makes it essential for everyone working in this field." (Christiane Albrecht, Analytical and Bioanalytical Chemistry, Vol. 390, 2008)Table of Contentsto Fluorescence.- Instrumentation for Fluorescence Spectroscopy.- Fluorophores.- Time-Domain Lifetime Measurements.- Frequency-Domain Lifetime Measurements.- Solvent and Environmental Effects.- Dynamics of Solvent and Spectral Relaxation.- Quenching of Fluorescence.- Mechanisms and Dynamics of Fluorescence Quenching.- Fluorescence Anisotropy.- Time-Dependent Anisotropy Decays.- Advanced Anisotropy Concepts.- Energy Transfer.- Time-Resolved Energy Transfer and Conformational Distributions of Biopolymers.- Energy Transfer to Multiple Acceptors in One,Two, or Three Dimensions.- Protein Fluorescence.- Time-Resolved Protein Fluorescence.- Multiphoton Excitation and Microscopy.- Fluorescence Sensing.- Novel Fluorophores.- DNA Technology.- Fluorescence-Lifetime Imaging Microscopy.- Single-Molecule Detection.- Fluorescence Correlation Spectroscopy.- Radiative Decay Engineering: Metal-Enhanced Fluorescence.- Radiative-Decay Engineering: Surface Plasmon-Coupled Emission.

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Book SynopsisProvides comprehensive coverage on using X-ray fluorescence for laboratory applications This book focuses on the practical aspects of X-ray fluorescence (XRF) spectroscopy and discusses the requirements for a successful sample analysis, such as sample preparation, measurement techniques and calibration, as well as the quality of the analysis results. X-Ray Fluorescence Spectroscopy for Laboratory Applications begins with a short overview of the physical fundamentals of the generation of X-rays and their interaction with the sample material, followed by a presentation of the different methods of sample preparation in dependence on the quality of the source material and the objective of the measurement. After a short description of the different available equipment types and their respective performance, the book provides in-depth information on the choice of the optimal measurement conditions and the processing of the measurement results. It covers instrument types for XRF; acquisition and evaluation of X-Ray spectra; analytical errors; analysis of homogeneous materials, powders, and liquids; special applications of XRF; process control and automation. An important resource for the analytical chemist, providing concrete guidelines and support for everyday analyses Focuses on daily laboratory work with commercially available devices Offers a unique compilation of knowledge and best practices from equipment manufacturers and users Covers the entire work process: sample preparation, the actual measurement, data processing, assessment of uncertainty, and accuracy of the obtained results X-Ray Fluorescence Spectroscopy for Laboratory Applications appeals to analytical chemists, analytical laboratories, materials scientists, environmental chemists, chemical engineers, biotechnologists, and pharma engineers.Trade ReviewX-ray fluorescence spectroscopy for laboratory applications is a strongly recommended, high-quality monograph in the field of X-ray spectroscopy. [?] [I]t is a unique resource for practitioners and scientists. Kerstin Leopold in Analytical and Bioanalytical Chemistry (29.07.2021)Table of ContentsPreface xvii List of Abbreviations and Symbols xix About the Authors xxiii 1 Introduction 1 2 Principles of X-ray Spectrometry 7 2.1 Analytical Performance 7 2.2 X-ray Radiation and Their Interaction 11 2.2.1 Parts of an X-ray Spectrum 11 2.2.2 Intensity of the Characteristic Radiation 13 2.2.3 Nomenclature of X-ray Lines 15 2.2.4 Interaction of X-rays with Matter 15 2.2.4.1 Absorption 16 2.2.4.2 Scattering 17 2.2.5 Detection of X-ray Spectra 20 2.3 The Development of X-ray Spectrometry 21 2.4 Carrying Out an Analysis 26 2.4.1 Analysis Method 26 2.4.2 Sequence of an Analysis 27 2.4.2.1 Quality of the Sample Material 27 2.4.2.2 Sample Preparation 27 2.4.2.3 Analysis Task 28 2.4.2.4 Measurement and Evaluation of the Measurement Data 28 2.4.2.5 Creation of an Analysis Report 29 3 Sample Preparation 31 3.1 Objectives of Sample Preparation 31 3.2 Preparation Techniques 32 3.2.1 Preparation Techniques for Solid Samples 32 3.2.2 Information Depth and Analyzed Volume 32 3.2.3 Infinite Thickness 36 3.2.4 Contaminations 37 3.2.5 Homogeneity 38 3.3 Preparation of Compact and Homogeneous Materials 39 3.3.1 Metals 39 3.3.2 Glasses 40 3.4 Small Parts Materials 41 3.4.1 Grinding of Small Parts Material 42 3.4.2 Preparation by Pouring Loose Powder into a Sample Cup 43 3.4.3 Preparation of the Measurement Sample by Pressing into a Pellet 44 3.4.4 Preparation of the Sample by Fusion Beads 48 3.4.4.1 Improving the Quality of the Analysis 48 3.4.4.2 Steps for the Production of Fusion Beads 49 3.4.4.3 Loss of Ignition 53 3.4.4.4 Quality Criteria for Fusion Beads 53 3.4.4.5 Preparation of Special Materials 54 3.5 Liquid Samples 55 3.5.1 Direct Measurement of Liquids 55 3.5.2 Special Processing Procedures for Liquid Samples 58 3.6 Biological Materials 58 3.7 Small Particles, Dust, and Aerosols 59 4 XRF Instrument Types 61 4.1 General Design of an X-ray Spectrometer 61 4.2 Comparison of Wavelength- and Energy-Dispersive X-Ray Spectrometers 63 4.2.1 Data Acquisition 63 4.2.2 Resolution 64 4.2.2.1 Comparison of Wavelength- and Energy-Dispersive Spectrometry 64 4.2.2.2 Resolution of WDS Instruments 66 4.2.2.3 Resolution of EDS Instruments 68 4.2.3 Detection Efficiency 70 4.2.4 Count Rate Capability 71 4.2.4.1 Optimum Throughput in ED Spectrometers 71 4.2.4.2 Saturation Effects in WDSs 72 4.2.4.3 Optimal Sensitivity of ED Spectrometers 73 4.2.4.4 Effect of the Pulse Throughput on the Measuring Time 74 4.2.5 Radiation Flux 75 4.2.6 Spectra Artifacts 76 4.2.6.1 Escape Peaks 76 4.2.6.2 Pile-Up Peak 77 4.2.6.3 Diffraction Peaks 77 4.2.6.4 Shelf and Tail 79 4.2.7 Mechanical Design and Operating Costs 79 4.2.8 Setting Parameters 80 4.3 Type of Instruments 80 4.3.1 ED Instruments 81 4.3.1.1 Handheld Instruments 82 4.3.1.2 Portable Instruments 83 4.3.1.3 Tabletop Instruments 84 4.3.2 Wavelength-Dispersive Instruments 85 4.3.2.1 Sequential Spectrometers 85 4.3.2.2 Multichannel Spectrometers 87 4.3.3 Special Type X-Ray Spectrometers 87 4.3.3.1 Total Reflection Instruments 88 4.3.3.2 Excitation by Monoenergetic Radiation 90 4.3.3.3 Excitation with Polarized Radiation 91 4.3.3.4 Instruments for Position-Sensitive Analysis 93 4.3.3.5 Macro X-Ray Fluorescence Spectrometer 94 4.3.3.6 Micro X-Ray Fluorescence with Confocal Geometry 95 4.3.3.7 High-Resolution X-Ray Spectrometers 96 4.3.3.8 Angle Resolved Spectroscopy – Grazing Incidence and Grazing Exit 96 4.4 Commercially Available Instrument Types 98 5 Measurement and Evaluation of X-ray Spectra 99 5.1 Information Content of the Spectra 99 5.2 Procedural Steps to Execute a Measurement 101 5.3 Selecting the Measurement Conditions 102 5.3.1 Optimization Criteria for the Measurement 102 5.3.2 Tube Parameters 103 5.3.2.1 Target Material 103 5.3.2.2 Excitation Conditions 104 5.3.2.3 Influencing the Energy Distribution of the Primary Spectrum 105 5.3.3 Measurement Medium 107 5.3.4 Measurement Time 108 5.3.4.1 Measurement Time and Statistical Error 108 5.3.4.2 Measurement Strategies 108 5.3.4.3 Real and Live Time 109 5.3.5 X-ray Lines 110 5.4 Determination of Peak Intensity 112 5.4.1 Intensity Data 112 5.4.2 Treatment of Peak Overlaps 112 5.4.3 Spectral Background 114 5.5 Quantification Models 117 5.5.1 General Remarks 117 5.5.2 Conventional Calibration Models 118 5.5.3 Fundamental Parameter Models 121 5.5.4 Monte Carlo Quantifications 124 5.5.5 Highly Precise Quantification by Reconstitution 124 5.5.6 Evaluation of an Analytical Method 126 5.5.6.1 Degree of Determination 126 5.5.6.2 Working Range, Limits of Detection (LOD) and of Quantification 127 5.5.6.3 Figure of Merit 129 5.5.7 Comparison of the Various Quantification Models 129 5.5.8 Available Reference Materials 131 5.5.9 Obtainable Accuracies 132 5.6 Characterization of Layered Materials 133 5.6.1 General Form of the Calibration Curve 133 5.6.2 Basic Conditions for Layer Analysis 135 5.6.3 Quantification Models for the Analysis of Layers 138 5.7 Chemometric Methods for Material Characterization 140 5.7.1 Spectra Matching and Material Identification 141 5.7.2 Phase Analysis 141 5.7.3 Regression Methods 143 5.8 Creation of an Application 143 5.8.1 Analysis of Unknown Sample Qualities 143 5.8.2 Repeated Analyses on Known Samples 144 6 Analytical Errors 149 6.1 General Considerations 149 6.1.1 Precision of a Measurement 151 6.1.2 Long-Term Stability of the Measurements 153 6.1.3 Precision and Process Capability 154 6.1.4 Trueness of the Result 156 6.2 Types of Errors 156 6.2.1 Randomly Distributed Errors 157 6.2.2 Systematic Errors 158 6.3 Accounting for Systematic Errors 159 6.3.1 The Concept of Measurement Uncertainties 159 6.3.2 Error Propagation 160 6.3.3 Determination of Measurement Uncertainties 161 6.3.3.1 Bottom-Up Method 161 6.3.3.2 Top-Down Method 162 6.4 Recording of Error Information 164 7 Other Element Analytical Methods 167 7.1 Overview 167 7.2 Atomic Absorption Spectrometry (AAS) 168 7.3 Optical Emission Spectrometry 169 7.3.1 Excitation with a Spark Discharge (OES) 169 7.3.2 Excitation in an Inductively Coupled Plasma (ICP-OES) 170 7.3.3 Laser-Induced Breakdown Spectroscopy (LIBS) 171 7.4 Mass Spectrometry (MS) 172 7.5 X-Ray Spectrometry by Particle Excitation (SEM-EDS, PIXE) 173 7.6 Comparison of Methods 175 8 Radiation Protection 177 8.1 Basic Principles 177 8.2 Effects of Ionizing Radiation on Human Tissue 178 8.3 Natural Radiation Exposure 179 8.4 Radiation Protection Regulations 181 8.4.1 Legal Regulations 181 9 Analysis of Homogeneous Solid Samples 183 9.1 Iron Alloys 183 9.1.1 Analytical Problem and Sample Preparation 183 9.1.2 Analysis of Pig and Cast Iron 184 9.1.3 Analysis of Low-Alloy Steel 185 9.1.4 Analysis of High-Alloy Steel 187 9.2 Ni–Fe–Co Alloys 188 9.3 Copper Alloys 189 9.3.1 Analytical Task 189 9.3.2 Analysis of Compact Samples 189 9.3.3 Analysis of Dissolved Samples 189 9.4 Aluminum Alloys 191 9.5 Special Metals 192 9.5.1 Refractories 192 9.5.1.1 Analytical Problem 192 9.5.1.2 Sample Preparation of Hard Metals 192 9.5.1.3 Analysis of Hard Metals 193 9.5.2 Titanium Alloys 194 9.5.3 Solder Alloys 194 9.6 Precious Metals 195 9.6.1 Analysis of Precious Metal Jewelry 195 9.6.1.1 Analytical Task 195 9.6.1.2 Sample Shape and Preparation 196 9.6.1.3 Analytical Equipment 197 9.6.1.4 Accuracy of the Analysis 198 9.6.2 Analysis of Pure Elements 198 9.7 Glass Material 199 9.7.1 Analytical Task 199 9.7.2 Sample Preparation 200 9.7.3 Measurement Equipment 202 9.7.4 Achievable Accuracies 202 9.8 Polymers 203 9.8.1 Analytical Task 203 9.8.2 Sample Preparation 204 9.8.3 Instruments 205 9.8.4 Quantification Procedures 205 9.8.4.1 Standard-Based Methods 205 9.8.4.2 Chemometric Methods 206 9.9 Abrasion Analysis 209 10 Analysis of Powder Samples 213 10.1 Geological Samples 213 10.1.1 Analytical Task 213 10.1.2 Sample Preparation 214 10.1.3 Measurement Technique 215 10.1.4 Detection Limits and Trueness 215 10.2 Ores 216 10.2.1 Analytical Task 216 10.2.2 Iron Ores 216 10.2.3 Mn, Co, Ni, Cu, Zn, and Pb Ores 217 10.2.4 Bauxite and Alumina 218 10.2.5 Ores of Precious Metals and Rare Earths 219 10.3 Soils and Sewage Sludges 221 10.3.1 Analytical Task 221 10.3.2 Sample Preparation 221 10.3.3 Measurement Technology and Analytical Performance 222 10.4 Quartz Sand 223 10.5 Cement 223 10.5.1 Analytical Task 223 10.5.2 Sample Preparation 224 10.5.3 Measurement Technology 225 10.5.4 Analytical Performance 226 10.5.5 Determination of Free Lime in Clinker 227 10.6 Coal and Coke 227 10.6.1 Analytical Task 227 10.6.2 Sample Preparation 228 10.6.3 Measurement Technology and Analytical Performance 229 10.7 Ferroalloys 230 10.7.1 Analytical Task 230 10.7.2 Sample Preparation 230 10.7.3 Analysis Technology 232 10.7.4 Analytical Performance 234 10.8 Slags 235 10.8.1 Analytical Task 235 10.8.2 Sample Preparation 235 10.8.3 Measurement Technology and Analytical Accuracy 236 10.9 Ceramics and Refractory Materials 237 10.9.1 Analytical Task 237 10.9.2 Sample Preparation 237 10.9.3 Measurement Technology and Analytical Performance 238 10.10 Dusts 239 10.10.1 Analytical Problem and Dust Collection 239 10.10.2 Measurement 242 10.11 Food 242 10.11.1 Analytical Task 242 10.11.2 Monitoring of Animal Feed 243 10.11.3 Control of Infant Food 244 10.12 Pharmaceuticals 245 10.12.1 Analytical Task 245 10.12.2 Sample Preparation and Analysis Method 245 10.13 Secondary Fuels 246 10.13.1 Analytical Task 246 10.13.2 Sample Preparation 247 10.13.2.1 Solid Secondary Raw Materials 247 10.13.2.2 Liquid Secondary Raw Materials 249 10.13.3 Instrumentation and Measurement Conditions 250 10.13.4 Measurement Uncertainties in the Analysis of Solid Secondary Raw Materials 251 10.13.5 Measurement Uncertainties for the Analysis of Liquid Secondary Raw Materials 252 11 Analysis of Liquids 253 11.1 Multielement Analysis of Liquids 254 11.1.1 Analytical Task 254 11.1.2 Sample Preparation 254 11.1.3 Measurement Technology 254 11.1.4 Quantification 255 11.2 Fuels and Oils 255 11.2.1 Analysis of Toxic Elements in Fuels 256 11.2.1.1 Measurement Technology 256 11.2.1.2 Analytical Performance 258 11.2.2 Analysis of Additives in Lubricating Oils 258 11.2.3 Identification of Abrasive Particles in Used Lubricants 260 11.3 Trace Analysis in Liquids 261 11.3.1 Analytical Task 261 11.3.2 Preparation by Drying 261 11.3.3 Quantification 262 11.4 Special Preparation Techniques for Liquid Samples 263 11.4.1 Determination of Light Elements in Liquids 263 11.4.2 Enrichment Through Absorption and Complex Formation 264 12 Trace Analysis Using Total Reflection X-Ray Fluorescence 267 12.1 Special Features of TXRF 267 12.2 Sample Preparation for TXRF 269 12.3 Evaluation of the Spectra 271 12.3.1 Spectrum Preparation and Quantification 271 12.3.2 Conditions for Neglecting the Matrix Interaction 272 12.3.3 Limits of Detection 273 12.4 Typical Applications of the TXRF 274 12.4.1 Analysis of Aqueous Solutions 274 12.4.1.1 Analytical Problem and Preparation Possibilities 274 12.4.1.2 Example: Analysis of a Fresh Water Standard Sample 275 12.4.1.3 Example: Detection of Mercury in Water 277 12.4.2 Analysis of the Smallest Sample Quantities 278 12.4.2.1 Example: Pigment Analysis 278 12.4.2.2 Example: Aerosol Analysis 279 12.4.2.3 Example: Analysis of Nanoparticles 279 12.4.3 Trace Element Analysis on Human Organs 280 12.4.3.1 Example: Analysis of Blood and Blood Serum 280 12.4.3.2 Example: Analysis of Trace Elements in Body Tissue 282 12.4.4 Trace Analysis of Inorganic and Organic Chemical Products 283 12.4.5 Analysis of Semiconductor Electronics 284 12.4.5.1 Ultra-Trace Analysis on SiWafers with VPD 284 12.4.5.2 Depth Profile Analysis by Etching 285 13 Nonhomogeneous Samples 287 13.1 Measurement Modes 287 13.2 Instrument Requirements 288 13.3 Data Evaluation 290 14 Coating Analysis 291 14.1 Analytical Task 291 14.2 Sample Handling 292 14.3 Measurement Technology 293 14.4 The Analysis Examples of Coated Samples 294 14.4.1 Single-Layer Systems: Emission Mode 294 14.4.2 Single-Layer Systems: Absorption Mode 297 14.4.3 Single-Layer Systems: Relative Mode 298 14.4.3.1 Analytical Problem 298 14.4.3.2 Variation of the Specified Working Distance 298 14.4.3.3 Sample Size and Spot Size Mismatch 299 14.4.3.4 Non-detectable Elements in the Layer: NiP Layers 300 14.4.4 Characterization of Ultrathin Layers 302 14.4.5 Multilayer Systems 304 14.4.5.1 Layer Systems 304 14.4.5.2 Measurement Technology 305 14.4.5.3 Example: Analysis of CIGS Solar Cells 305 14.4.5.4 Example: Analysis of Solder Structures 306 14.4.6 Samples with Unknown Coating Systems 307 14.4.6.1 Preparation of Cross Sections 308 14.4.6.2 Excitation at Grazing Incidence with Varying Angles 309 14.4.6.3 Measurement in Confocal Geometry 311 15 Spot Analyses 313 15.1 Particle Analyses 313 15.1.1 Analytical Task 313 15.1.2 Sample Preparation 314 15.1.3 Analysis Technology 315 15.1.4 Application Example:Wear Particles in Used Oil 315 15.1.5 Application Example: Identification of Glass Particles by Chemometrics 316 15.2 Identification of Inclusions 318 15.3 Material Identification with Handheld Instruments 318 15.3.1 Analytical Tasks 318 15.3.2 Analysis Technology 319 15.3.3 Sample Preparation and Test Conditions 320 15.3.4 Analytical Accuracy 320 15.3.5 Application Examples 321 15.3.5.1 Example: Lead in Paint 321 15.3.5.2 Example: Scrap Sorting 321 15.3.5.3 Example: Material Inspection and Sorting 322 15.3.5.4 Example: Precious Metal Analysis 322 15.3.5.5 Example: Prospecting and Screening in Geology 323 15.3.5.6 Example: Investigation of Works of Art 323 15.4 Determination of Toxic Elements in Consumer Products: RoHS Monitoring 324 15.4.1 Analytical Task 324 15.4.2 Analysis Technology 325 15.4.3 Analysis Accuracy 327 15.5 Toxic Elements in Toys: Toys Standard 328 15.5.1 Analytical Task 328 15.5.2 Sample Preparation 328 15.5.3 Analysis Technology 330 16 Analysis of Element Distributions 331 16.1 General Remarks 331 16.2 Measurement Conditions 332 16.3 Geology 333 16.3.1 Samples Types 333 16.3.2 Sample Preparation and Positioning 333 16.3.3 Measurements on Compact Rock Samples 334 16.3.3.1 Sum Spectrum and Element Distributions 334 16.3.3.2 Object Spectra 335 16.3.3.3 Treatment of Line Overlaps 336 16.3.3.4 Maximum Pixel Spectrum 339 16.3.4 Thin Sections of Geological Samples 340 16.4 Electronics 342 16.5 Archeometric Investigations 344 16.5.1 Analytical Tasks 344 16.5.2 Selection of an Appropriate Spectrometer 346 16.5.3 Investigations of Coins 347 16.5.4 Investigations of Painting Pigments 349 16.6 Homogeneity Tests 350 16.6.1 Analytical Task 350 16.6.2 Homogeneity Studies Using Distribution Analysis 351 16.6.3 Homogeneity Studies Using Multi-point Measurements 352 17 Special Applications of the XRF 355 17.1 High-Throughput Screening and Combinatorial Analysis 355 17.1.1 High-Throughput Screening 355 17.1.2 Combinatorial Analysis for Drug Development 357 17.2 Chemometric Spectral Evaluation 358 17.3 High-Resolution Spectroscopy for Speciation Analysis 361 17.3.1 Analytical Task 361 17.3.2 Instrument Technology 361 17.3.3 Application Examples 362 17.3.3.1 Analysis of Different Sulfur Compounds 362 17.3.3.2 Speciation of Aluminum Inclusions in Steel 363 17.3.3.3 Determination of SiO2 in SiC 365 18 Process Control and Automation 367 18.1 General Objectives 367 18.2 Off-Line and At-Line Analysis 369 18.2.1 Sample Supply and Analysis 369 18.2.2 Automated Sample Preparation 371 18.3 In-Line and On-Line Analysis 376 19 Quality Management and Validation 379 19.1 Motivation 379 19.2 Validation 380 19.2.1 Parameters 384 19.2.2 Uncertainty 385 Appendix A Tables 387 Appendix B Important Information 419 B.1 Coordinates of Main Manufacturers of Instruments and Preparation Tools 419 B.2 Main Suppliers of Standard Materials 422 B.2.1 Geological Materials and Metals 422 B.2.2 Stratified Materials 423 B.2.3 Polymer Standards 424 B.2.4 High Purity Materials 424 B.2.5 Precious Metal Alloys 425 B.3 Important Websites 425 B.3.1 Information About X-Ray Analytics and Fundamental Parameters 425 B.3.2 Information About Reference Materials 426 B.3.3 Scientific Journals 427 B.4 Laws and Acts, Which Are Important for X-Ray Fluorescence 427 B.4.1 Radiation Protection 427 B.4.2 Regulations for Environmental Control 428 B.4.3 Regulations for Performing Analysis 428 B.4.4 Use of X-ray Fluorescence for the Chemical Analysis 428 B.4.4.1 General Regulations 428 B.4.4.2 Analysis of Minerals 429 B.4.4.3 Analysis of Oils, Liquid Fuels, Grease 430 B.4.4.4 Analysis of Solid Fuels 432 B.4.4.5 Coating Analysis 433 B.4.4.6 Metallurgy 433 B.4.4.7 Analysis of Electronic Components 434 References 435 Index 453

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Book SynopsisThis book is a well-established guide to the interpretation of the mass, ultraviolet, infrared and nuclear magnetic resonance spectra of organic compounds. It is designed for students of organic chemistry taking a course in the application of these techniques to structure determination. The text also remains useful as a source of data for organic chemists to keep on their desks throughout their career. In the seventh edition, substantial portions of the text have been revised reflecting knowledge gained during the author's teaching experience over the last seven years. The chapter on NMR has been divided into two separate chapters covering the 1D and 2D experiments. The discussion is also expanded to include accounts of the physics at a relatively simple level, following the development of the magnetization vectors as each pulse sequence is introduced. The emphasis on the uses of NMR spectroscopy in structure determination is retained. Worked examples and problem sets are included on a chapter level to allow students to practise their skills by determining the chemical structures of unknown compounds.Table of ContentsChapter 1: Mass spectra 1.1 Introduction 1.2 Ion production 1.2.1 Electron impact (EI) 1.2.2 Chemical Ionisation (CI) 1.2.3 Electrospray ionisation (ESI) 1.2.4 Fast ion bombardment (FIB or LSIMS) 1.2.5 Laser desorption (LD) and matrix-assisted laser desorption (MALDI) 1.3 Ion analysis 1.3.1 Magnetic analysers 1.3.2 Time-of–flight (TOF) analysers 1.3.3 Quadrupole analysers 1.3.4 Ion cyclotron resonance (ICR) analysers 1.3.5 Ion-trap analysers 1.4 Structural information from EI mass spectra 1.4.1 The features of an EI spectrum 1.4.2 The molecular ion 1.4.3 Isotopic abundances 1.4.4 Identifying the molecular ion 1.4.5 Fragmentation in EI spectra 1.5 Fragmentation in CI and FIB spectra 1.5.1 Fragmentation in CI spectra 1.5.2 Fragmentation in FIB (LSMIS) spectra 1.6 Some examples of mass spectrometry in action 1.6.1 San Joaquin oil 1.6.2 Oleic acid 1.6.3 The oviposition pheromone 1.6.4 Identifying antibodies 1.6.5 The ESI spectra of melittin and the human parathyroid hormone 1.6.6 ESI-FT-ICR and ESI-FT-Orbitrap spectra 1.7 Separation coupled to mass spectrometry 1.7.1 GC/MS and LC/MS 1.7.2 MS/MS 1.8 Interpreting the spectrum of an unknown 1.9 Internet 1.10 Bibliography 1.11 Problems 1.12 Tables of data Chapter 2: Ultraviolet and visible spectra 2.1 Introduction 2.2 Chromophores 2.3 The absorption laws 2.4 Measurement of the spectrum 2.5 Vibrational fine structure 2.6 Selection rules and intensity 2.7 Solvent effects 2.8 Searching for a chromophore 2.9 Definitions 2.10 Conjugated dienes 2.11 Polyenes and poly-ynes 2.12 Ketones and aldehydes; p®p* transitions 2.13 Ketones and aldehydes; n®p* transitions 2.14 a,b-Unsaturated acids, esters, nitriles and amides 2.15 Aromatic compounds 2.16 Quinones 2.17 Corroles, chlorins and porphyrins 2.18 Non-conjugated interacting chromophores 2.19 The effect of steric hindrance to coplanarity 2.20 Internet 2.21 Bibliography 2.22 Problems Chapter 3: Infrared spectra 3.1 Introduction 3.2 Preparation of samples and examination in an infrared spectrometer 3.3 Selection rules 3.4 The infrared spectrum 3.5 The use of the tables of characteristic group frequencies 3.6 Stretching frequencies of single bonds to hydrogen 3.7 Stretching frequencies of triple and cumulated double bonds 3.8 Stretching frequencies in the double-bond region 3.9 Characteristic vibrations of aromatic rings 3.10 Groups absorbing in the fingerprint region 3.11 Raman spectra 3.12 Internet 3.13 Bibliography 3.14 Problems 3.15 Correlation charts 3.16 Tables of data Chapter 4: 1D-NMR spectra 4.1 Nuclear spin and resonance 4.2 Taking a spectrum 4.3 The chemical shift 4.4 Factors affecting the chemical shift 4.4.1 The inductive effect 4.4.2 Anisotropy of chemical bonds 4.4.3 Polar effects of conjugation 4.4.4 Van der Waals forces 4.4.5 Isotope effects 4.4.6 Estimating a chemical shift 4.4.7 Hydrogen bonds 4.4.8 Solvent effects and temperature 4.5 Spin-spin coupling to 13C 4.5.1 13C-2H Coupling 4.5.2 13C-1H Coupling 4.5.3 13C-13C Coupling 4.6 1H-1H Coupling—multiplicity and coupling patterns 4.6.1 1H-1H Vicinal coupling (3JHH) 4.6.2 AB systems 4.6.3 1H-1H Geminal coupling (2JHH) 4.6.4 1H-1H Long-range coupling (4JHH and 5JHH) 4.6.5 Deviations from first-order coupling 4.7 1H-1H Coupling—the magnitude of coupling constants 4.7.1 The sign of coupling constants 4.7.2 Vicinal coupling (3JHH) 4.7.3 Geminal coupling (2JHH) 4.7.4 Long-range coupling (4JHH and 5JHH) 4.7.5 C–H coupling (1JCH, 2JCH and 3JCH) 4.8 Coupling from 1H and 13C to 19F and 31P 4.8.1 13C NMR spectra of compounds containing 19F and 31P 4.8.2 1H NMR spectra of compounds containing 19F and 31P 4.9 Relaxation and its consequences 4.9.1 Longitudinal relaxation 4.9.2 Transverse relaxation and exchange 4.10 Improving the NMR spectrum 4.10.1 The effect of changing the magnetic field 4.10.2 Solvent effects 4.10.3 Shift reagents 4.11 Spin decoupling 4.11.1 Simple spin decoupling 4.11.2 Difference decoupling 4.12 Identifying spin systems—1D-TOCSY 4.13 The nuclear Overhauser effect 4.13.1 Origins 4.13.2 NOE-Difference spectra 4.14 The rotating frame of reference 4.15 Assignment of CH3, CH2, CH and fully substituted carbons in 13C NMR 4.15.1 The Attached Proton Test (APT) 4.15.2 DEPT 4.16 Hints for structure determination using 1D-NMR 4.16.1 Carbon spectra 4.16.2 Proton spectra 4.17 Further information 4.17.1 The internet 4.17.2 Bibliography 4.18 Tables of data Chapter 5: 2D-NMR spectra 5.1 The basic pulse sequence 5.2 COSY 5.2.1 Cross peaks from scalar coupling 5.2.2 Polarisation transfer 5.2.3 The origin of cross peaks 5.2.4 Displaying COSY spectra 5.2.5 Interpreting COSY spectra 5.2.6 Axial peaks 5.2.7 Gradient pulses 5.2.8 DQF-COSY 5.2.9 Phase structure in COSY spectra 5.3 2D-TOCSY 5.4 NOESY 5.5 Cross-correlated 2D spectra identifying 1-bond connections 5.5.1 Heteronuclear Multiple Quantum Coherence (HMQC) spectra 5.5.2 Heteronuclear Single Quantum Coherence (HSQC) spectra 5.5.3 Examples of HSQC spectra 5.5.4 Non-uniform sampling (NUS) 5.5.5 Cross-peak detail—determining the sign of coupling constants 5.5.6 CLIP-HSQC 5.5.7 Deconvoluting a 1H spectrum using the HSQC spectrum 5.5.8 HSQC-TOCSY 5.5.9 HETCOR 5.6 Cross-correlated 2D spectra identifying 2- and 3-bond connections 5.6.1 The HMBC pulse sequence 5.6.2 HMBC spectra 5.7 Some specialised NMR techniques 5.7.1 ADEQUATE—identifying 13C-13C connections 5.7.2 INADEQUATE—identifying 13C-13C connections 5.7.3 HSQC-HECADE—measuring the sign and magnitude of 13C-1H coupling constants 5.8 Three- and four-dimensional NMR 5.9 Hints for structure determination using 2D-NMR 5.10 Bibliography 5.11 Table of information Chapter 6: Worked examples in structure determination 6.1 General approach 6.2 Simple worked examples using 13C NMR alone 6.3 Simple worked examples using 1H NMR alone 6.4 Simple worked examples using the combined application of MS, UV, IR and 1D-NMR spectroscopic methods 6.5 Simple worked examples using the combined application of MS, UV, IR and 1D-NMR and 2D-NMR spectroscopic methods Chapter 7: Problem sets 7.1 Chemical shift problems 7.2 1D-NMR chemical shift and coupling problems 7.3 Problems using all the spectroscopic methods Answers to problems 1-34 Index

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Book SynopsisTable of Contents1. Introduction 2. Introducing High-Resolution NMR 3. Practical Aspects of High-Resolution NMR 4. One-Dimensional Techniques 5. Introducing Two-Dimensional and Pulsed Field Gradient NMR 6. Correlations Through the Chemical Bond I: Homonuclear Shift Correlation 7. Correlations Through the Chemical Bond II: Heteronuclear Shift Correlation 8. Separating Shifts and Couplings: J-Resolved and Pure Shift Spectroscopy 9. Correlations Through Space: The Nuclear Overhauser Effect 10. Diffusion NMR Spectroscopy 11. Protein–Ligand Screening by NMR 12. Experimental Methods 13. Structure Elucidation and Spectrum Assignment

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Book SynopsisRepresents practical spectroscopic methodology, reviews, and information for organic materials, surfactants, and polymer spectra covering the ultraviolet, visible, near infrared, infrared, Raman and dielectric measurement techniques. This work includes description of interpretive and chemometric techniques used for spectral data analysis.Trade Review"This Handbook can provide a valuable reference for the daily activities of students and professionals working in modern molecular spectroscopy laboratories. Any one of them, when faced with a problem could take great comfort from the knowledge that this handbook wan on his bookshelf. The Handbook contains valuable material that shoul make a substantial contribution towards aiding spectral interpretation and data processing of organic spectra, polymers, and surfactants." --CURRENT ENGINEERING PRACTICE, HANDBOOK OF MACHINERY DYNAMICS, Vol.43, Nos 2-3; July-August-Septemeber, 2000; October-November-December, 2000 "the reviewers...highly recommend this book to analytical chemists, industrial chemists, and serious spectroscopists. Although the cost is high, the value is also high. Nowhere else is such a compilation of data, techniques, references, and general spectroscopic information available. Despite the minor flaws, this is a must-have book." --SPECTROSCOPY MAGAZINE

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Book SynopsisNuclear magnetic resonance (NMR) spectroscopy, a technique widely used for structure determination by chemists and biochemists, is based on the detection of tiny radio signals emitted by the nucleus of an atom when immersed in a strong magnetic field. Every chemical substance gives rise to a recognizable NMR signature closely related to its molecular structure. This comprehensive account adopts an accessible, pictorial approach to teach the fundamental principles of high resolution NMR. Mathematical formalism is used sparingly, and everyday analogies are used to provide insight into the physical behaviour of nuclear spins. The first three chapters set out the basic tools for understanding the rest of the book. Each of the remaining chapters provides a self- contained reference to a specific theme, for example spin echoes, and traces the way it influences our understanding of high resolution NMR methodology. Spin Choreography provides a clear and an authoritative introduction to the funTable of Contents1. Energy levels ; 2. Vector model ; 3. Product operator formalism ; 4. Spin echoes ; 5. Soft radiofrequency pulses ; 6. Separating the wheat from the chaff ; 7. Broadband decoupling ; 8. Two-dimensional spectroscopy ; 9. Nuclear Overhauser effect ; 10. In defence of noise ; 11. Water ; 12. Measurement of coupling constants

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Book SynopsisThis is the first book devoted to the use of X-ray beam techniques to study magnetic properties of materials. It covers both experimental and theoretical issues. The three main topics are dichroism, elastic scattering (both non-resonant and resonant diffraction) and spectroscopy.Trade ReviewThis book provides a thorough introduction to both experimental and theretical issues that arise in investigations of materials using the methods of X-ray scattering and absorption * Zeitschrift fur Kristallographie *this monograph, addressing researchers in the field in an elegant, civilised but unpretentious and occasionally idiosyncratic style and vocabulary, sets a high standard for a proposed series on synchrotron radiation * Contemporary Physics Vol. 38 No.5 1997 *Firstly, it is suitable for anyone who would like to become acquainted with a new field of spectroscopy that has made sensational progress over the past decade and, secondly, it is a valuable reference book for those who are already familiar with the techniques... The first part incorporates a great deal of recent work along with many useful tips for the experimentalist and will be readily appreciated by the non-specialist reader... The strength and merit of this book is that both experimental and theoretical issues have been addressed and have been skilfully interwoven. In addition, although magnetic scattering is in the early stages of development, the book establishes a foundation on which further research can be built. * Journal of Synchrotron Radiation, vol. 5, part 3, May 1998 *It must surely play a part in raising the awareness of researchers in magnetism in the potential value of synchrotron-based techniques. The book is suitable for graduate students and researchers with an interest in magnetic materials and for professionals who wish to consider the use of synchrotron radiation in their research... It is surely an indispensable item for the university and the institutional library. * Journal of Synchrotron Radiation, vol. 5, part 3, May 1998 *Table of Contents1. Introductory survey ; 2. Non-resonant magentic X-ray diffraction from antiferromagnets ; 3. Non-resonant magnetic diffraction from ferromagnets ; 4. Magnetic X-ray dichroism ; 5. Resonant X-ray diffraction from antiferromagnets ; 6. Resonant magnetic X-ray diffraction from ferromagnets ; 7. Compton scattering ; 8. Theoretical framework ; Appendix ; Index

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Book SynopsisThe renowned Oxford Chemistry Primer series, which provides focused introductions to a range of important topics in chemistry, has been refreshed and updated to suit the needs of today''s students, lecturers, and postgraduate researchers. The rigorous, yet accessible, treatment of each subject area is ideal for those wanting a primer in a given topic to prepare them for more advanced study or research. Moreover, cutting-edge examples and applications throughout the texts show the relevance of the chemistry being described to current research and industry. The learning features provided, including questions at the end of every chapter and online multiple-choice questions, encourage active learning and promote understanding. Furthermore, frequent diagrams, margin notes, further reading, and glossary definitions all help to enhance a student''s understanding of these essential areas of chemistry. Foundations of Molecular Structure Determination covers a range of common spectroscopic and dTable of Contents1. Overview, energy levels and the electromagnetic spectrum ; 2. Rotational and vibrational spectroscopy ; 3. Electronic (ultraviolet-visible) absorption spectroscopy ; 4. Nuclear magnetic resonance spectroscopy ; 5. Mass spectrometry ; 6. X-ray diffraction and related methods

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Book SynopsisChemical imaging has a variety of applications for almost every facet of our daily lives, ranging from medical diagnosis and treatment to the study and design of material properties in new products. This book reviews the state of chemical imaging technology, identifies promising future developments and their applications, and more.Table of Contents1 Front Matter; 2 Executive Summary; 3 1 Introduction; 4 2 Utilizing Chemical Imaging to Address Scientific and Technical Challenges: Case Studies; 5 3 Imaging Techniques: State of the Art and Future Potential; 6 4 Committee Findings and Recommendations; 7 A Statement of Task; 8 B Committee Member Biographies; 9 C Guest Panelists; 10 D Acronyms and Abbreviations

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Book SynopsisThis book introduces the subject of impedance spectroscopy starting from fundamentals through to latest applications in areas such as ceramics, piezoelectric, sensors, agriculture, food quality control, medical diagnostics, cancer research, and so forth. Within the ambit of impedance spectroscopy, plots simulated for useful equivalent circuit models, design of sample holder, necessary precautions to be taken during measurement are described. It further discusses development of softwares for analysis of experimental data and choice of the most appropriate equivalent circuit model. All the materials are supported by problems, answers, appendices and references.Features: Includes fundamentals, equivalent circuit modeling and analysis of data related to impedance spectroscopy. Presents experimental measurements in a nuts-and-bolts approach. Includes derivation of expressions for some selected models and values of immittance functions as frequency oTable of Contents1. Basic Ideas. 2. Concept of Impedance Spectroscopy, Various Immittance Functions and Equivalent Circuit Representation. 3. Experimental Measurements. 4. Equivalent Circuit Models and Their Simulated Immittance Behaviors. 5. Analysis of Experimental Data. 6. Applications.

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Book SynopsisThis book offers concise information on the properties of polymeric materials, particularly those most relevant to physical chemistry and chemical physics. Extensive updates and revisions to each chapter include eleven new chapters on novel polymeric structures, reinforcing phases in polymers, and experiments on single polymer chains.Trade ReviewFrom the reviews of the second edition: "This edition of Physical Properties of Polymers Handbook is a mammoth undertaking with 63 chapters divided into nine parts and 100 distinguished contributors with affiliations in industry, academia, and governmental agencies. The objectives of the book are very ambitious. … The compilations of physical properties are very readable and, depending on one’s interests, range from the mundane and practical to the esoteric. … All in all, this is a very useful compendium and should have a place on every polymer scientist’s bookshelf." (George Christopher Martin, Journal of the American Chemical Society, Vol. 130 (3), 2008) "This handbook covers an enormous range of properties of polymeric materials, particularly those relevant to the areas of physical chemistry and chemical physics. … It is a reference work for researchers or advanced students studying polymeric materials. … The main goal of the book is to discuss and describe important results and modern developments. … If the reader … wishes to work in polymer applications or related areas, this is a good book to have available." (Christian Brosseau, Optics and Photonics News, February, 2008)Table of ContentsPreface to the Second Edition. -Preface to the First Edition. -STRUCTURE. -Chain Structures. -Names, Acronyms, Classes, and Structures of Some Important Polymers. -THEORY. -The Rotational Isomeric State Model. -Computational Parameters. -Theoretical Models and Simulations of Polymer Chains. -Scaling, Exponents, and Fractal Dimensions. -THERMODYNAMIC PROPERTIES. -Densities, Coefficients of Thermal Expansion, and Compressibilities of Amorphous Polymers. -Thermodynamic Properties of Proteins. -Heat Capacities of Polymers. -Thermal Conductivity. -Thermodynamic Quantities Governing Melting. -The Glass Temperature. -Sub-Tg Transitions. -Polymer-Solvent Interaction Parameter c. -Theta Temperatures. -Solubility Parameters. -Mark-Houwink-Staudinger-Sakurada Constants. -Polymers and Supercritical Fluids. -Thermodynamics of Polymer Blends. -SPECTROSCOPY. -NMR Spectroscopy of Polymers. -Broadband Dielectric Spectroscopy to Study the Molecular Dynamics of Polymers Having Different Molecular Architectures. -Group Frequency Assignments for Major Infrared Bands Observed in Common Synthetic Polymers. -Small Angle Neutron and X-Ray Scattering. -MECHANICAL PROPERTIES. -Mechanical Properties. -Chain Dimensions and Entanglement Spacings. -Temperature Dependences of the Viscoelastic Response of Polymer Systems. -Adhesives. -Some Mechanical Properties of Typical Polymer-Based Composites. -Polymer Networks and Gels. -Force Spectroscopy of Polymers: Beyond Single Chain Mechanics. -REINFORCING PHASES. -Carbon Black. -Properties of Polymers Reinforced with Silica. -Physical Properties of Polymer/Clay Nanocomposites. -Polyhedral Oligomeric Silsesquioxane (POSS). -Carbon Nanotube Polymer Composites: Recent Developments in Mechanical Properties. -Reinforcement Theories. -CRYSTALLINITY AND MORPHOLOGY. -Densities of Amorphous and Crystalline Polymers. -Unit Cell Information on Some Important Polymers. -Crystallization Kinetics of Polymers. -Block Copolymer Melts. -Polymer Liquid Crystals and Their Blends. -The Emergence of a New Macromolecular Architecture: 'The Dendritic State'. –Polyrotaxanes. -Foldamers: Nanoscale Shape Control at the Interface Between Small Molecules and High Polymers. -Recent Advances in Supramolecular Polymers. -ELECTRO-OPTICAL AND MAGNETIC PROPERTIES. -Conducting Polymers: Electrical Conductivity. -Conjugated Polymer Electroluminescence. -Magnetic, Piezoelectric, Pyroelectric, and Ferroelectric Properties of Synthetic and Biological Polymers. -Nonlinear Optical Properties of Polymers. -Refractive Index, Stress-Optical Coefficient, and Optical Configuration Parameter of Polymers. -RESPONSES TO RADIATION, HEAT, AND CHEMICAL AGENTS. -Ultraviolet Radiation and Polymers. -The Effects of Electron Beam and g-Irradiation on Polymeric Materials. –Flammability. -Thermal-Oxidative Stability and Degradation of Polymers. -Synthetic Biodegradable Polymers for Medical Applications. -Biodegradability of Polymers. -Properties of Photoresist Polymers. -Pyrolyzability of Preceramic Polymers. -OTHER PROPERTIES. -Surface and Interfacial Properties. -Acoustic Properties. -Permeability of Polymers to Gases and Vapors. –MISCELLANEOUS. –Definitions. -Units and Conversion Factors. -Subject Index

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Book SynopsisThe latest edition of a highly successful textbook, Mass Spectrometry, Third Edition provides students with a complete overview of the principles, theories and key applications of modern mass spectrometry. All instrumental aspects of mass spectrometry are clearly and concisely described: sources, analyzers and detectors.Trade Review"This is a great book for everyone in the field to keep handy." (CHOICE, April 2008) "Overview of the principles, theories, and key applications of modern mass spectrometry." (Materials and Corrosion, November 2007)Table of ContentsPreface xi Introduction 1 Principles 1 Diagram of a Mass Spectrometer 4 History 5 Ion Free Path 10 1 Ion Sources 15 1.1 Electron Ionization 15 1.2 Chemical Ionization 17 1.2.1 Proton transfer 19 1.2.2 Adduct formation 21 1.2.3 Charge-transfer chemical ionization 21 1.2.4 Reagent gas 22 1.2.5 Negative ion formation 25 1.2.6 Desorption chemical ionization 27 1.3 Field Ionization 28 1.4 Fast Atom Bombardment and Liquid Secondary Ion Mass Spectrometry 29 1.5 Field Desorption 31 1.6 Plasma Desorption 32 1.7 Laser Desorption 33 1.8 Matrix-Assisted Laser Desorption Ionization 33 1.8.1 Principle of MALDI 33 1.8.2 Practical considerations 36 1.8.3 Fragmentations 39 1.8.4 Atmospheric pressure matrix-assisted laser desorption ionization 39 1.9 Thermospray 41 1.10 Atmospheric Pressure Ionization 42 1.11 Electrospray 43 1.11.1 Multiply charged ions 46 1.11.2 Electrochemistry and electric field as origins of multiply charged ions 48 1.11.3 Sensitivity to concentration 50 1.11.4 Limitation of ion current from the source by the electrochemical process 51 1.11.5 Practical considerations 54 1.12 Atmospheric Pressure Chemical Ionization 55 1.13 Atmospheric Pressure Photoionization 56 1.14 Atmospheric Pressure Secondary Ion Mass Spectrometry 61 1.14.1 Desorption electrospray ionization 61 1.14.2 Direct analysis in real time 62 1.15 Inorganic Ionization Sources 65 1.15.1 Thermal ionization source 65 1.15.2 Spark source 67 1.15.3 Glow discharge source 68 1.15.4 Inductively coupled plasma source 69 1.15.5 Practical considerations 71 1.16 Gas-Phase Ion-Molecule Reactions 72 1.17 Formation and Fragmentation of Ions: Basic Rules 76 1.17.1 Electron ionization and photoionization under vacuum 77 1.17.2 Ionization at low pressure or at atmospheric pressure 77 1.17.3 Proton transfer 77 1.17.4 Adduct formation 78 1.17.5 Formation of aggregates or clusters 79 1.17.6 Reactions at the interface between source and analyser 79 2 Mass Analysers 85 2.1 Quadrupole Analysers 88 2.1.1 Description 88 2.1.2 Equations of motion 91 2.1.3 Ion guide and collision cell 96 2.1.4 Spectrometers with several quadrupoles in tandem 98 2.2 Ion Trap Analysers 100 2.2.1 The 3D ion trap 100 2.2.2 The 2D ion trap 117 2.3 The Electrostatic Trap or ‘Orbitrap’ 122 2.4 Time-of-Flight Analysers 126 2.4.1 Linear time-of-flight mass spectrometer 126 2.4.2 Delayed pulsed extraction 129 2.4.3 Reflectrons 131 2.4.4 Tandem mass spectrometry with time-of-flight analyser 134 2.4.5 Orthogonal acceleration time-of-flight instruments 139 2.5 Magnetic and Electromagnetic Analysers 143 2.5.1 Action of the magnetic field 143 2.5.2 Electrostatic field 144 2.5.3 Dispersion and resolution 145 2.5.4 Practical considerations 146 2.5.5 Tandem mass spectrometry in electromagnetic analysers 149 2.6 Ion Cyclotron Resonance and Fourier Transform Mass Spectrometry 157 2.6.1 General principle 157 2.6.2 Ion cyclotron resonance 159 2.6.3 Fourier transform mass spectrometry 159 2.6.4 MSn in ICR/FTMS instruments 164 2.7 Hybrid Instruments 164 2.7.1 Electromagnetic analysers coupled to quadrupoles or ion trap 165 2.7.2 Ion trap analyser combined with time-of-flight or ion cyclotron resonance 166 2.7.3 Hybrids including time-of-flight with orthogonal acceleration 167 3 Detectors and Computers 175 3.1 Detectors 175 3.1.1 Photographic plate 176 3.1.2 Faraday cup 176 3.1.3 Electron multipliers 177 3.1.4 Electro-optical ion detectors 181 3.2 Computers 182 3.2.1 Functions 183 3.2.2 Instrumentation 183 3.2.3 Data acquisition 183 3.2.4 Data conversion 186 3.2.5 Data reduction 186 3.2.6 Library search 186 4 Tandem Mass Spectrometry 189 4.1 Tandem Mass Spectrometry in Space or in Time 189 4.2 Tandem Mass Spectrometry Scan Modes 192 4.3 Collision-Activated Decomposition or Collision-Induced Dissociation 195 4.3.1 Collision energy conversion to internal energy 196 4.3.2 High-energy collision (keV) 198 4.3.3 Low-energy collision (between 1 and 100 eV) 199 4.4 Other Methods of Ion Activation 199 4.5 Reactions Studied in MS/MS 202 4.6 Tandem Mass Spectrometry Applications 204 4.6.1 Structure elucidation 205 4.6.2 Selective detection of target compound class 207 4.6.3 Ion–molecule reaction 210 4.6.4 The kinetic method 211 5 Mass Spectrometry/Chromatography Coupling 217 5.1 Elution Chromatography Coupling Techniques 218 5.1.1 Gas chromatography/mass spectrometry 219 5.1.2 Liquid chromatography/mass spectrometry 221 5.1.3 Capillary electrophoresis/mass spectrometry 228 5.2 Chromatography Data Acquisition Modes 228 5.3 Data Recording and Treatment 230 5.3.1 Data recording 230 5.3.2 Instrument control and treatment of results 232 6 Analytical Information 243 6.1 Mass Spectrometry Spectral Collections 243 6.2 High Resolution 245 6.2.1 Information at different resolving powers 249 6.2.2 Determination of the elemental composition 251 6.3 Isotopic Abundances 251 6.4 Low-mass Fragments and Lost Neutrals 257 6.5 Number of Rings or Unsaturations 258 6.6 Mass and Electron Parities, Closed-shell Ions and Open-shell Ions 259 6.6.1 Electron parity 259 6.6.2 Mass parity 259 6.6.3 Relationship between mass and electron parity 260 6.7 Quantitative Data 260 6.7.1 Specificity 260 6.7.2 Sensitivity and detection limit 262 6.7.3 External standard method 264 6.7.4 Sources of error 265 6.7.5 Internal standard method 266 6.7.6 Isotopic dilution method 268 7 Fragmentation Reactions 273 7.1 Electron Ionization and Fragmentation Rates 273 7.2 Quasi-Equilibrium and RRKM Theory 275 7.3 Ionization and Appearance Energies 279 7.4 Fragmentation Reactions of Positive Ions 280 7.4.1 Fragmentation of odd-electron cations or radical cations (OE•+) 280 7.4.2 Fragmentation of cations with an even number of electrons (EE+) 286 7.4.3 Fragmentations obeying the parity rule 288 7.4.4 Fragmentations not obeying the parity rule 291 7.5 Fragmentation Reactions of Negative Ions 291 7.5.1 Fragmentation mechanisms of even electron anions (EE–) 292 7.5.2 Fragmentation mechanisms of radical anions (OE•−) 293 7.6 Charge Remote Fragmentation 293 7.7 Spectrum Interpretation 294 7.7.1 Typical ions 296 7.7.2 Presence of the molecular ion 296 7.7.3 Typical neutrals 296 7.7.4 A few examples of the interpretation of mass spectra 298 8 Analysis of Biomolecules 305 8.1 Biomolecules and Mass Spectrometry 305 8.2 Proteins and Peptides 306 8.2.1 ESI and MALDI 307 8.2.2 Structure and sequence determination using fragmentation 309 8.2.3 Applications 324 8.3 Oligonucleotides 342 8.3.1 Mass spectra of oligonucleotides 343 8.3.2 Applications of mass spectrometry to oligonucleotides 346 8.3.3 Fragmentation of oligonucleotides 351 8.3.4 Characterization of modified oligonucleotides 355 8.4 Oligosaccharides 357 8.4.1 Mass spectra of oligosaccharides 358 8.4.2 Fragmentation of oligosaccharides 360 8.4.3 Degradation of oligosaccharides coupled with mass spectrometry 367 8.5 Lipids 371 8.5.1 Fatty acids 373 8.5.2 Acylglycerols 376 8.5.3 Bile acids 382 8.6 Metabolomics 386 8.6.1 Mass spectrometry in metabolomics 387 8.6.2 Applications 388 9 Exercises 403 Questions 403 Answers 415 Appendices 437 1 Nomenclature 437 1.1 Units 437 1.2 Definitions 437 1.3 Analysers 438 1.4 Detection 439 1.5 Ionization 440 1.6 Ion types 441 1.7 Ion–molecule reaction 442 1.8 Fragmentation 442 2 Acronyms and abbreviations 442 3 Fundamental Physical Constants 446 4A Table of Isotopes in Ascending Mass Order 447 4B Table of Isotopes in Alphabetical Order 452 5 Isotopic Abundances (in %) for Various Elemental Compositions CHON 457 6 Gas-Phase Ion Thermochemical Data of Molecules 467 7 Gas-Phase Ion Thermochemical Data of Radicals 469 8 Literature on Mass Spectrometry 470 9 Mass Spectrometry on Internet 476 Index 479

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Book SynopsisAn essential reference for optical sensor system design This is the first text to present an integrated view of the optical and mathematical analysis tools necessary to understand computational optical system design. It presents the foundations of computational optical sensor design with a focus entirely on digital imaging and spectroscopy.Trade Review?Designed for advanced undergraduate and graduate courses in optical sensor design, and as a reference for sensor designers in radio and millimeter wave, X- ray, and acoustic systems, Brady's is the first text to present an integrated view of the optical and mathematical analysis tools necessary to understand computational optical system design.? ( Book News, September 2009)Table of ContentsPreface. Acknowledgments. 1. Past, present and future. 1.1 Three revolutions. 1.2 Computational imaging. 1.3 Overview. 1.4 The fourth revolution. Problems. 2. Geometric imaging. 2.1 Visibility. 2.2 Optical elements. 2.3 Focal imaging. 2.4 Imaging systems. 2.5 Pinhole and coded aperture imaging. 2.6 Projection tomography. 2.7 Reference structure tomography. Problems. 3. Analysis. 3.1 Analytical tools. 3.2 Fields and transformations. 3.3 Fourier analysis. 3.4 Transfer functions and filters. 3.5 The Fresnel transformation. 3.6 The Whittaker-Shannon sampling theorem. 3.7 Discrete analysis of linear transformations. 3.8 Multiscale sampling. 3.9 B-splines. 3.10 Wavelets. Problems. 4. Wave imaging. 4.1 Waves and fields. 4.2 Wave model for optical fields. 4.3 Wave propagation. 4.4 Diffraction. 4.5 Wave analysis of optical elements. 4.6 Wave propagation through thin lenses. 4.7 Fourier analysis of wave imaging. 4.8 Holography. Problems. 5. Detection. 5.1 The Optoelectronic interface. 5.2 Quantum mechanics of optical detection. 5.3 Optoelectronic detectors. 5.3.1 Photoconductive detectors. 5.3.2 Photodiodes. 5.4 Physical characteristics of optical detectors. 5.5 Noise. 5.6 Charge coupled devices. 5.7 Active pixel sensors. 5.8 Infrared focal plane arrays. Problems. 6. Coherence imaging. 6.1 Coherence and spectral fields. 6.2 Coherence propagation. 6.3 Measuring coherence. 6.4 Fourier analysis of coherence imaging. 6.5 Optical coherence tomography. 6.6 Modal analysis. 6.7 Radiometry. Problems. 7. Sampling. 7.1 Samples and pixels. 7.2 Image plane sampling on electronic detector arrays. 7.3 Color imaging. 7.4 Practical sampling models. 7.5 Generalized sampling. Problems. 8. Coding and inverse problems. 8.1 Coding taxonomy. 8.2 Pixel coding. 8.3 Convolutional coding. 8.4 Implicit coding. 8.5 Inverse problems. Problems. 9. Spectroscopy. 9.1 Spectral measurements. 9.2 Spatially dispersive spectroscopy. 9.3 Coded aperture spectroscopy. 9.4 Interferometric Spectroscopy. 9.5 Resonant spectroscopy. 9.6 Spectroscopic filters. 9.7 Tunable filters. 9.8 2D spectroscopy. Problems. 10. Computational imaging. 10.1 Imaging systems. 10.2 Depth of field. 10.3 Resolution. 10.4 Multiple aperture imaging. 10.5 Generalized sampling revisited. 10.6 Spectral imaging. Problems. References.

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Book SynopsisConfidently face the challenges of proteomics research specific to plant science with the information in Plant Proteomics, which will introduce you to the techniques and methodologies required for the study of representative plant species. Read about proteomics studies in Arabidopsis, rice, and legumes and find information about common technologies like mass spectrometry and gel electrophoresis. Discover expression proteomics, functional proteomics, structural proteomics, bioinformatics, and systems biology, understand how to conduct proteomics studies in developing countries and underfunded laboratories, and gain access to guidelines for sample preparation.Table of ContentsPREFACE. CONTRIBUTORS. ACRONYMS AND ABBREVIATIONS. 1. AN INTRODUCTION TO PROTEOMICS: APPLICATIONS TO PLANT BIOLOGY (Ralph A. Bradshaw). PART I: TECHNOLOGIES. 2. GEL-BASED PROTEOMICS (Pier Giorgio Righetti, Paolo Antonioli, Carolina Simo, and Attilio Citterio). 3. MASS SPECTROMETRY-BASED PROTEOMICS: IDENTIFYING PLANT PROTEINS (Eveline Bergmuller, Sacha Baginsky, and Wilhelm Gruissem). 4. CHEMICAL PROTEOMICS (Miriam C. Hagenstein, Olaf Kruse, and Norbert Sewald). 5. THE ARABIDOPSIS LOCALIZOME: SUBCELLULAR PROTEIN LOCALIZATION AND INTERACTIONS IN ARABIDOPSIS (Georgios Kitsios, Nicolas Tsesmetzis, Max Bush, and John H. Doonan). 6. SECRETOME: TOWARD DECIPHERING THE SECRETORY PATHWAYS AND BEYOND (Young-Ho Jung, Ganesh Kumar Agrawal, Randeep Rakwal, and Nam-Soo Jwa). 7. PEPTIDOMICS (Peter Schulz-Knappe). PART II: COMPUTATIONAL PROTEOMICS. 8. BIOINFORMATICS IN GEL-BASED PROTEOMICS (Asa M. Wheelock and Craig E. Wheelock). 9. BIOINFORMATICS IN MS-BASED PROTEOMICS (Jacques Colinge). PART III: EXPRESSION PROTEOMICS. 10. AN OVERVIEW OF THE ARABIDOPSIS PROTEOME (Jacques Bourguignon and Michel Jaquinod). 11. RICE PROTEOME AT A GLANCE (Ganesh Kumar Agrawal and Randeep Rakwal). 12. PROTEOMICS OF LEGUME PLANTS (Satish Nagaraj, Zhentian Lei, Bonnie Watson, and Lloyd W. Sumner). 13. PROTEOME OF SEED DEVELOPMENT AND GERMINATION (Julie Catusse, Loıc Rajjou, Claudette Job, and Dominique Job). 14. ENDOSPERM AND AMYLOPLAST PROTEOMES OF WHEAT GRAIN (William J. Hurkman, William H. Vensel, Frances M. DuPont, Susan B. Altenbach, and Bob B. Buchanan). 15. ROOT PROTEOME (Kuo-Chen Yeh, Chyi-Chuann Chen, and Chuan-Ming Yeh). 16. LEAF PROTEOME (Bin Kang, Shuyang Tu, Jiyuan Zhang, and Siqi Liu). 17. ANTHER PROTEOME (Nijat Imin). 18. POLLEN PROTEOME (Sandra Noir). 19. MICROTUBULE-BINDING PROTEINS (Lori A. Vickerman and Douglas G. Muench). PART IV: ORGANELLE PROTEOMICS. 20. CELL WALL (Elisabeth Jamet, Herv´e Canut, Cecile Albenne, Georges Boudart, and Rafael Pont-Lezica). 21. PLASMA MEMBRANE: A PECULIAR STATUS AMONG THE CELL MEMBRANE SYSTEMS (Geneviève Ephritikhine, Anne Marmagne, Thierry Meinnel, and Myriam Ferro). 22. NUCLEUS (Subhra Chakraborty, Aarti Pandey, Asis Datta, and Niranjan Chakraborty). 23. CHLOROPLAST (Thomas Kieselbach and Wolfgang P. Schröder). 24. ETIOPLAST (Anne von Zychlinski, Sonja Reiland, Wilhelm Gruissem, and Sacha Baginsky). 25. THE PLANT MITOCHONDRIAL PROTEOME AND THE CHALLENGE OF HYDROPHOBIC PROTEIN ANALYSIS (Yew-Foon Tan and A. Harvey Millar). 26. PEROXISOME (Yuko Arai, Youichiro Fukao, Makoto Hayashi, and Mikio Nishimura). 27. UNRAVELING PLANT VACUOLES BY PROTEOMICS (Songqin Pan and Natasha Raikhel). 28. OIL BODIES (Pascale Jolivet, Luc Negroni, Sabine d’Andrea, and Thierry Chardot). PART V: MODIFICATION PROTEOMICS. 29. PHOSPHOPROTEINS: WHERE ARE WE TODAY? (Florian Wolschin and Wolfram Weckwerth). 30. PROTEOME ANALYSIS OF THE UBIQUITIN PATHWAY (Junmin Peng). 31. ANALYSIS OF THE N-GLYCOSYLATION OF PROTEINS IN PLANTS (Willy Morelle). 32. FUNCTIONAL ANALYSIS AND PHOSPHORYLATION SITE MAPPING OF LEUCINE-RICH REPEAT RECEPTOR-LIKE KINASES (Steven D. Clouse, Michael B. Goshe, Steven C. Huber, and Jia Li). 33. TIME TO SEARCH FOR PROTEIN KINASE SUBSTRATES (Birgit Kersten). 34. TYROSINE PHOSPHORYLATION IN PLANTS: EMERGING EVIDENCE (Andrea Carpi, Valeria Rossi, and Francesco Filippini). 35. 14–3–3 PROTEINS: REGULATORS OF KEY CELLULAR FUNCTIONS (Peter C. Morris). PART VI: MULTIPROTEIN COMPLEX. 36. TAP-TAGGING SYSTEM IN RICE FOR PROTEIN COMPLEX ISOLATION (Jai S. Rohila and Michael E. Fromm). 37. TAP STRATEGY IN ARABIDOPSIS PROTEIN COMPLEX ISOLATION (Vicente Rubio and Xing Wang Deng). 38. BLUE-NATIVE PAGE IN STUDYING PROTEIN COMPLEXES (Holger Eubel and A. Harvey Millar). 39. PROTEIN–PROTEIN INTERACTION MAPPING IN PLANTS (Joachim F. Uhrig). PART VII: PLANT DEFENSE AND STRESS. 40. PROTEOMICS IN PLANT DEFENSE RESPONSE (Sun Tae Kim and Kyu Young Kang). 41. PROTEOME ANALYSIS OF CELLULAR RESPONSES TO ABIOTIC STRESSES IN PLANTS (Hans-Peter Mock and Andrea Matros). 42. PROTEOMICS OF BIOTROPHIC PLANT–MICROBE INTERACTIONS: SYMBIOSES LEAD THE MARCH (Ghislaine Recorbet and Eliane Dumas-Gaudot). 43. PROTEOMICS APPROACHES TO CONSTRUCT CALCIUM SIGNALING NETWORKS IN PLANTS (Irene S. Day and A.S.N. Reddy). PART VIII: STRUCTURAL PROTEOMICS. 44. CELL-FREE EXPRESSION SYSTEM FOR EUKARYOTIC PROTEINS (Yaeta Endo and Tatsuya Sawasaki). 45. PROTEIN STRUCTURE DETERMINATION (Jian-Hua Zhao and Hsuan-Liang Liu). PART IX: OTHER TOPICS IN PLANT PROTEOMICS. 46. PROTEOMICS IN CONTEXT OF SYSTEMS BIOLOGY (Serhiy Souchelnytskyi). 47. PROTEOMICS IN DEVELOPING COUNTRIES (Nat N. V. Kav, Sanjeeva Srivastava, William Yajima, and Shakir Ali). INDEX.

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Book SynopsisWith chapters provided by international leading experts, this book covers the recent advances in protein and peptide mass spectrometry.Trade Review"This book will be a valuable reference as it contains plenty of depth and substance to be of interest to experienced practitioners of mass spectrometry and related techniques, but is still accessible to pharmaceutical researchers who want to learn more about MS technologies and its applications." (American Society for Mass Spectrometry, 1 July 2012) Table of ContentsPREFACE xv CONTRIBUTORS xvii PART I METHODOLOGY 1 1 Ionization Methods in Protein Mass Spectrometry 3 Ismael Cotte-Rodriguez, Yun Zhang, Zhixin Miao, and Hao Chen 1.1 History of the Development of Protein Mass Spectrometry 4 1.2 Laser-Based Ionization Methods for Proteins 5 1.3 Spray-Based Ionization Methods for Proteins 13 1.4 Ambient Ionization Methods 20 1.5 Conclusions 30 Acknowledgments 30 References 30 2 Ion Activation and Mass Analysis in Protein Mass Spectrometry 43 Cheng Lin and Peter O’Connor 2.1 Introduction 43 2.2 Ion Activation and Tandem MS Analysis 46 2.3 Mass Analyzers 59 References 81 3 Target Proteins: Bottom-up and Top-down Proteomics 89 Michael Boyne and Ron Bose 3.1 Mass Spectral Approaches to Targeted Protein Identification 89 3.2 Bottom-up Proteomics 90 3.3 Top-down Approaches 96 3.4 Next-Generation Approaches 98 References 99 4 Quantitative Proteomics by Mass Spectrometry 101 Jacob Galan, Anton Iliuk, and W. Andy Tao 4.1 Introduction 101 4.2 In-Cell Labeling 105 4.3 Quantitation via Isotopic Labeling of Proteins 107 4.4 Quantitation via Isotopic Labeling on Peptides 112 4.5 Label-Free Quantitation 116 4.6 Conclusions 119 Acknowledgment 120 References 120 5 Comparative Proteomics by Direct Tissue Analysis Using Imaging Mass Spectrometry 129 Michelle L. Reyzer and Richard M. Caprioli 5.1 Introduction 129 5.2 Conventional Comparative Proteomics 130 5.3 Comparative Proteomics Using Imaging MS 131 5.4 Conclusions 136 Acknowledgments 137 References 137 6 Peptide and Protein Analysis Using Ion Mobility–Mass Spectrometry 139 Jeffrey R. Enders, Michal Kliman, Sevugarajan Sundarapandian, and John A. McLean 6.1 Ion Mobility–Mass Spectrometry: Instrumentation and Separation Selectivity 139 6.2 Characterizing and Interpreting Peptide and Protein Structures 147 6.3 Applications of IM-MS to Peptide and Protein Characterizations 152 6.4 Future Directions 158 Acknowledgments 159 References 160 7 Chemical Footprinting for Determining Protein Properties and Interactions 175 Sandra A. Kerfoot and Michael L. Gross 7.1 Introduction to Hydrogen–Deuterium Exchange 175 7.2 Experimental Procedures 178 7.3 Mass Spectrometry-Based HDX in Practice 182 7.4 Protein Footprinting via Free-Radical Oxidation 193 7.5 Chemical Crosslinking 198 7.6 Selective and Irreversible Chemical Modification 201 7.7 Conclusion 205 References 206 8 Microwave Technology to Accelerate Protein Analysis 213 Urooj A. Mirza, Birendra N. Pramanik, and Ajay K. Bose 8.1 Introduction 213 8.2 Microwave Technology 215 8.3 Summary 224 Acknowledgments 224 References 224 9 Bioinformatics and Database Searching 231 Surendra Dasari and David L. Tabb 9.1 Overview 231 9.2 Introduction to Tandem Mass Spectrometry 231 9.3 Overview of Peptide Identification with Database Searching 234 9.4 MyriMatch-IDPicker Protein Identification Pipeline 235 9.5 Results of a Shotgun Proteomics Study 246 9.6 Improvements to MyriMatch Database Search Engine 248 9.7 Applications of MyriMatch-IDPicker Pipeline 250 9.8 Conclusions 251 Acknowledgments 251 References 251 PART II Applications 253 10 Mass Spectrometry-Based Screening and Characterization of Protein–Ligand Complexes in Drug Discovery 255 Christine L. Andrews, Michael R. Ziebell, Elliott Nickbarg, and Xianshu Yang 10.1 Introduction 255 10.2 Affinity Selection Mass Spectrometry (AS-MS) 256 10.3 Solution-Based AS-MS as Screening Technologies 258 10.4 Gas-Phase Interactions 267 10.5 Enzyme Activity Assays Using MS for Screening or Confirming Drug Candidates 271 10.6 Conclusions and Future Directions 276 References 277 11 Utilization of Mass Spectrometry for the Structural Characterization of Biopharmaceutical Protein Products 287 Amareth Lim and Catherine A. Srebalus Barnes 11.1 Introduction 287 11.2 MS-Based Approach for the Characterization of Recombinant Therapeutic Proteins 288 11.3 Cell Culture Development 290 11.4 Purification Development 294 11.5 Formulation Development 300 11.6 Analytical Method Development 304 11.7 Confirmation of Structure/Product Comparability Assessment 311 11.8 Conclusions 313 Acknowledgments 315 References 315 12 Post-translationally Modified Proteins: Glycosylation, Phosphorylation, and Disulfide Bond Formation 321 Anthony Tsarbopoulos and Fotini N. Bazoti 12.1 Introduction 321 12.2 Glycosylation 322 12.3 Phosphorylation 338 12.4 Disulfide Bond Detection and Mapping 347 12.5 Future Perspectives 350 Acknowledgments 352 Abbreviations 353 References 354 13 Mass Spectrometry of Antigenic Peptides 371 Henry Rohrs 13.1 Introduction 371 13.2 Analysis of Antigenic Peptides 374 13.3 Examples of the Application of Mass Spectrometry to Antigenic Peptide Study 381 13.4 Future Work 385 Acknowledgments 386 Abbreviations 387 References 387 14 Neuropeptidomics 393 Jonathan V. Sweedler, Fang Xie, and Adriana Bora 14.1 Introduction 393 14.2 Neuropeptidomics: Characterizing Peptides in the Brain 394 14.3 Sample Preparation for Mass Spectrometry 395 14.4 Separations 405 14.5 Peptide Characterization via Mass Spectrometry 407 14.6 Conclusions 419 14.7 Future Perspectives 419 Acknowledgments 420 References 420 15 Mass Spectrometry for the Study of Peptide Drug Metabolism 435 Patrick J. Rudewicz 15.1 Introduction 435 15.2 Peptide Drug Metabolism 436 15.3 LC-MS/MS for Metabolite Identification 437 15.4 Quantitative Analysis 439 15.5 Case Study: IL-1b Protease Inhibitors 440 15.6 Future Directions 445 References 445 INDEX 449

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Book SynopsisMass spectrometry (MS) is a crucial method in ensuring the production, quality, and safety of grape, wine, and grape-derivative products. This book concisely presents the applications of mass spectrometry in the analysis of wine, from traditional to more recent developments.Trade Review"This book is very suitable for any scientist working in the oenological field who uses MS for the development of analytical methods or who wants to determine which mass technology is the most appropriate for his/her analytical problem ." (Anal Bioanal Chem, 2010) "So in summary, an excellent book is edited very well by Riccardo Flamini and Pietro Traldi and written by real experts in the field of mass spectrometry and wine chemistry." (Chromatographia, 6 March 2011) Table of ContentsPreface. Acknowledgments. Introduction. PART I: MASS SPECTROMETRY. 1 Ionization Methods. 1.1. Electrospray Ionization. 1.2. Atmospheric Pressure Chemical Ionization. 1.3. Atmospheric Pressure Photoionization. 1.4. Surface-Activated Chemical Ionization. 1.5. Matrix-Assisted Laser. References. 2 Mass Analyzers and Accurate Mass Measurements. 2.1. Double-Focusing Mass Analyzers. 2.2. Quadrupole Mass Filters. 2.3. Ion Traps. 2.4. Time of Flight. References. 3. MS/MS Methodologies. 3.1. Triple Quadrupole. 3.2. The Q-TOF. 3.3. The MALDI TOF-TOF. References. PART II: APPLICATIONS OF MASS SPECTROMETRY IN GRAPE AND WINE CHEMSITRY. 4 Grape Aroma Compounds: Terpenes, C13-Norisopenoids, Benzene Compounds, and 3-Alkyl-2-Methoxypyrazines. 4.1. Introduction. 4.2. The SPE-GC/MS of Terpenes, Norisoprenoids and Benzenoids. 4.3. The SPME-GC/MS of Methoxypyrazines in Juice and Wine. References. 5 Volatile and Aroma Compounds in Wines. 5.1. Higher Alcohols and Esters Formed from Yeasts. 5.2. Volatile Sulfur Compounds in Wines. 5.3. Carbonyl Compounds in Wines and Distillates. 5.4. Ethyl and Vinyl Phenols in Wines. 5.5. 2'-Aminoacetophenone in Wines. References. 6 Grape and Wine Polyphenols. 6.1. Introduction. 6.2. The LC/MS of Non-Anthocyanic Polyphenols of Grape. 6.3. The LC/MS of Non-Anthocyanic Polyphenols of Wine. 6.4. Liquid-Phase MS of Grape Anthocyanins. 6.5. The LC/MS of Anthocynanis Derivatives in Wine. 6.6. The MALDI-TOF of Grape Procyanidins. References. 7 Compounds Released in Wine from Wood. 7.1. Introduction. 7.2. The GC/MS of Wood Volatile Compounds. 7.3. The GC/PICI-MS/MS of Wood Volatile Phenols and Benzene Aldehydes in Wine. References. 8 Compounds Responsible for Wine Defects. 8.1. Ochratoxin A in Grape and Wine. 8.2. The SPME-GC/MS/MS Analysis of TCA and TBA in Wine. 8.3. Geosmin. 8.4. Analysis of 1-Octen-3-one. 8.5. Analysis of 2-Methoxy-3,5-dimethypyrazine in Wine. 8.6. Biogenic Amines in Grape and Wine. 8.7. Ethyl Carbamate in Wine. 8.8. Wine Geranium Taint. 8.9. Mousy Off-Flavor of Wines. References. 9 Pesticides in Grape and Wine. 9.1. Introduction. 9.2. Analytical Methods. 9.3. Isothiocyanates in Wine. References. 10 Peptides and Proteins of Grape and Wine. 10.1. Introduction. 10.2. Analytical Methods. References. Index.

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Book SynopsisA guide to spectroscopy and inorganic materials. It introduces the different optical spectroscopic techniques, used in many laboratories, for material characterisation. It also meets the demand from academia and the science community for an introductory text.Trade Review"This is a useful book for an undergraduate or an early-stage postgraduate course in spectroscopy." (Reviews, June 2008) "[allows] students with a background in quantum physics and solid state physics, to interpret simple optical spectra…and obtain knowledge of the main instrumentation used in this field." (Chimie Nouvelle, March 2007)Table of ContentsPREFACE. ACKNOWLEDGEMENTS. SOME PHYSICAL CONSTANTS OF INTEREST IN SPECTROSCOPY. I FUNDAMENTALS. I.1 Origin of the Spectroscopy. I.2 Electromagnetic Spectrum. Optical Spectroscopy. I.3 Absorption. The Spectrophotometer. I.4 Luminescence. The Spectrofluorimeter. Time resolved luminescence. I.5 Scattering. The Raman effect. I.6 Advanced topic: The Fourier Transform Spectrophotometer. Exercises. II LIGHT SOURCES. II.1 Introduction. II.2 Lamps. II.3 The Laser. Basic principles. II.4 Types of Lasers. II.5 Tunability of laser radiation. The Optical Parametric Oscillator. II.6 Advanced Topic:1) Site Selective Spectroscopy. 2) Excited State Absorption. Exercises. III MONOCHROMATORS AND DETECTORS. III.1 Introduction. III.2 Monochromators. III.3 Types of detectors. Basic parameters. III.4 The Photomultiplier. III.5 Signal/noise ratio optimisation. III.6 Detection of pulses. III.7 Advanced Topic: Detection of very fast pulses; The Streak Camera; The Correlator. Exercises. IV. OPTICAL TRANSPARENCY OF SOLIDS. IV.1 Introduction. IV.2 Optical magnitudes and the dielectric constant. IV.3The Lorentz oscillator. IV.4 Metals. IV.5 Semiconductors and insulators. IV.6 Spectral shape of the fundamental absorption edge. IV.7 Excitons. IV.8 Advanced topic: The colour of metals. Exercises. V. OPTICALLY ACTIVE CENTRES. V.1 Introduction. V.2 Static interaction. The crystalline field. V.3 Band intensities. The oscillator strength. V.4 Dynamic interaction. The coordinate configuration diagram. V.5 Band shape. The Huang-Rhys factor. V.6 Non radiative transitions. Energy transfer. V.7 Advanced topic: Determination of quantum efficiencies. Exercises. VI. APPLICATIONS: RARE EARTH AND TRANSITION METAL IONS, COLOUR CENTERS. VI.1 Introduction. VI.2 Trivalent rare earth ions. Diagram of Dieke. VI.3 Non radiative transitions in rare earth ions; The "energy gap" law. VI.4 Transition metal ions. Tanabe- Sugano diagrams. VI.5 Colour centres. VI.6 Advanced topic: 1) The Judd and Ofelt method. 2) Optical cooling of solids. Exercises. VII. GROUP THEORY AND SPECTROSCOPY. VII.1 Introduction. VII.2 Symmetry operations and classes. VII.3 Representations. The character table. VII.4 Reduction in symmetry and splitting of energy levels. VII.5 Selection rules for optical transitions. VII.6 Illustrative examples. VII.7 Advanced topic: Applications to optical transitions of Kramers ions. Exercises. APPENDICES. APPENDIX A1.- The joint density of states. APPENDIX A2.- Effect of an octahedral field on a valence electron d1. APPENDIX A3.- Calculation of the spontaneous emission probability by the Einstein thermodynamic treatment. APPENDIX A4.- Determination of the Smakula´s formula. INDEX.

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Book SynopsisFacilitates the discovery and development of new, effective therapeutics With coverage of the latest mass spectrometry technology, this book explains how mass spectrometry can be used to enhance almost all phases of drug discovery and drug development, including new and emerging applications. The book''s fifteen chapters have been written by leading pharmaceutical and analytical scientists. Their contributions are based on a thorough review of the current literature as well as their own experience developing new mass spectrometry techniques to improve the ability to discover and develop new and effective therapeutics. Mass Spectrometry for Drug Discovery and Drug Development begins with an overview of the types of mass spectrometers that facilitate drug discovery and development. Next it covers: HPLC?high-resolution mass spectrometry for quantitative assays Mass spectrometry for siRNA Quantitative analysis of peptides <Table of ContentsContributors ix Preface xi 1 Overview of the Various Types of Mass Spectrometers that are Used in Drug Discovery and Drug Development 1 Gérard Hopfgartner 2 Utility of High-Resolution Mass Spectrometry for New Drug Discovery Applications 37 William Bart Emary and Nanyan Rena Zhang 3 Quantitative Mass Spectrometry Considerations in a Regulated Environment 55 Mohammed Jemal and Yuan-Qing Xia 4 Mass Spectrometry for Quantitative In Vitro ADME Assays 97 Jun Zhang and Wilson Z. Shou 5 Metabolite Identifi cation Using Mass Spectrometry in Drug Development 115 Natalia Penner, Joanna Zgoda-Pols, and Chandra Prakash 6 MS Analysis of Biological Drugs, Proteins, and Peptides 149 Yi Du, John Mehl, and Pavlo Pristatsky 7 Characterization of Impurities and Degradation Products in Small Molecule Pharmaceuticals and Biologics 191 Hui Wei, Guodong Chen, and Adrienne A. Tymiak 8 Liquid Extraction Surface Analysis (LESA): A New Mass Spectrometry-Based Technique for Ambient Surface Profiling 221 Daniel Eikel and Jack D. Henion 9 MS Applications in Support of Medicinal Chemistry Sciences 239 Maarten Honing, Benno Ingelse, and Birendra N. Pramanik 10 Imaging Mass Spectrometry of Proteins and Peptides 277 Michelle L. Reyzer and Richard M. Caprioli 11 Imaging Mass Spectrometry for Drugs and Metabolites 303 Stacey R. Oppenheimer 12 Screening Reactive Metabolites: Role of Liquid Chromatography–High-Resolution Mass Spectrometry in Combination with “Intelligent” Data Mining Tools 339 Shuguang Ma and Swapan K. Chowdhury 13 Mass Spectrometry of siRNA 357 Mark T. Cancilla and W. Michael Flanagan 14 Mass Spectrometry for Metabolomics 387 Petia Shipkova and Michael D. Reily 15 Quantitative Analysis of Peptides with Mass Spectrometry: Selected Reaction Monitoring or High-Resolution Full Scan? 403 Lieve Dillen and Filip Cuyckens Index 427

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Book SynopsisA single-source reference describing how and why gas chromatography and mass spectrometry instruments work. Describes a wide range of technologies and offers guidance for their optimum use, outlining good practice, routine procedures, and trouble shooting.Table of ContentsGC/MS SYSTEMS AND COMPONENTS. Vacuum Systems. Mass Spectrometers. Gas Chromatography. GC/MS Interfacing. Data Systems. ROUTINE GC/MS OPERATION, TECHNIQUES, AND PROCEDURES. Gas Chromatography Methods and Techniques Relevant to GC/MS. Mass Spectrometer Operation. Laboratory Practice. Preventive Maintenance. TROUBLESHOOTING FAULTS ON GC/MS SYSTEMS. The GC/MS Instrument Under Fault Conditions. Fault Finding and Nonroutine Maintenance. CHOOSING A GC/MS SYSTEM. Instrument Selection and Evaluation. Bibliography. Index.

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Book SynopsisGraphite Furnace Atomic Absorption Spectrometry (GFAAS) is an established analytical laboratory technique used to examine materials in their vapor state by atomizing the sample in a graphite furnace. This approach is used mostly in the materials science and environmental analysis to examine alloys, polymers, ceramics, composites, and wastewater.Table of ContentsTheory. Quantitative GFAAS: Calibration. Instrumentation. Interference-Free Analysis. Sample Preparation and Introduction. Practical Hints on the Determination of Elements by GFAAS. Commercial GFAAS Instrumentation: Types, Costs, and Training. Future of GFAAS. Appendices. Index.

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Book SynopsisPacked with reviews plus new results from the author''s laboratories, the first-of-its-kind work offers a timely and authoritative treatise on the use of mass spectral techniques in organic stereochemistry. Featuring 22 chapters contributed by eminent and active researchers in the field, this unique sourcebook offers comparative information on the use of a variety of mass-spectral techniques to characterize stereoisomers and conformers of both large and small biologically important organic molecules. It also discusses techniques for studying gas-phase conformational equilibria in conformationally mobil systems. Applications of Mass Spectrometry to Organic Stereochemistry will dramatically aid the lab applications of organic, biological, pharmaceutical, and analytical chemists in university and industrial laboratories.Table of ContentsFrom the Contents: Mass Spectrometric Techniques/ Mass-Spectral Intermediate-Ion Structures/ Stereochemical Effects in the Fragmentation Processes of Saturated and Unsaturated Acyclic Molecular Ions/ Hidden Stereochemistry in the Fragmentation/ Processes of Saturated Cyclic Molecular Ions with One or Two Atoms Between the Functional Group and the Ring/ Stereochemical Effectsin the Fragmentation Processes/ Stereochemical Effects in the Retro-Diels-Alder Fragmentation/ Stereochemical Effects in Mass Spectra and Thermochemistry/ Stereochemical Effects in the Positive- and Negative-Ion Chemical-Ionization Mass Spectra of Stereoisomeric Molecules/ Stereochemical Effects in Ion-Molecule Reactions Studied by Ion-Cyclotron-Resonance Spectroscopy/ Stereochemical Effects in the Mass Spectra of Terpenes and Terpenoids/ Stereochemical Effects Observed for Steroid Compounds

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Book SynopsisX-ray fluorescence (XRF) and x-ray diffraction (XRD) are analytical techniques used to identify substances by examining the amount of energy given off from a substance during an x-ray. The most common errors in XRF analysis and XRD usually occur during preparation of the specimen.Table of ContentsSpecimen Preparation Procedures in X-Ray Fluorescence Analysis. Specimen Preparation in X-Ray Fluorescence. Specimen Preparation in X-Ray Diffraction. Specific Areas of Specimen Preparation in X-Ray Powder Diffraction. Special Problems in the Preparation of X-Ray Diffraction Specimens. Specimen Preparation for Camera Methods. Specimen Preparation Equipment. Use of Standards in X-Ray Fluorescence Analysis. Glossary. Bibliography. Index.

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Book SynopsisE = mc2 and the Periodic Table . . . RELATIVISTIC EFFECTS IN CHEMISTRY This century''s most famous equation, Einstein''s special theory of relativity, transformed our comprehension of the nature of time and matter. Today, making use of the theory in a relativistic analysis of heavy molecules, that is, computing the properties and nature of electrons, is the work of chemists intent on exploring the mysteries of minute particles. The first work of its kind, Relativistic Effects in Chemistry details the computational and analytical methods used in studying the relativistic effects in chemical bonding as well as the spectroscopic properties of molecules containing very heavy atoms. The first of two independent volumes, Part A: Theory and Techniques describes the basic techniques of relativistic quantum chemistry. Its systematic five-part format begins with a detailed exposition of Einstein''s special theory of relativity, the significance of relativitTrade Review"This book represents an invaluable source in relativistic quantum chemistry and is recommended warmly to anyone with an interest in this area . . .it fills a gap in the literature that has existed far too long."-- -- Chemistry in BritainTable of ContentsSpecial Relativity. Relativistic Quantum Mechanics. Relativistic Quantum Chemistry. Double-Group Symmetry and the Classification of Relativistic Electronic States. Index.

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Book SynopsisThe latest in a series providing chemical physicists with a forum for critical, authoritative evaluations of advances in every area of the discipline, this stand-alone volume focuses on using high resolution molecular spectroscopy to arrive at global and accurate Vibration Hamiltonians.Table of ContentsThe Forward Trip: From the Hamiltonian to the Vibration-Rotation Spectrum. The Backward Trip: From the Vibration-Rotation Data to the Hamiltonian. Experimental Overtone Spectroscopy. Acknowledgments. References. Appendices. Indexes.

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Book SynopsisLC-MS has become an indispensable tool for problem solving in virtually all analytical fields and is particularly useful for the separation and indentification of complex mixtures or organic/biological compounds.Trade Review"...should significantly enhance...understanding of the selected topic..." (THES Textbook Guide, 27 Feb 2004)Table of ContentsSeries Preface. Preface. Acknowledgements. Abbreviations, Acronyms and Symbols. About the Author. Introduction. Liquid Chromatography. Mass Spectrometry. Interface Technology. Applications of High Performance Liquid Chromatography - Mass Spectrometry. Responses to Self-Assessment Questions. Bibliography. Glossary of Terms. SI Units and Physical Constants. Periodic Table. Index.

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Book SynopsisMas spec identification simplified and streamlined While mass spectroscopy is an important tool for identifying unknown compounds, identifying the actual spectra can be laborious and time-consuming until now. The Important Peak Index of the Registry of Mass Spectral Data contains the same information as the Registry, but organized differently for easier navigation. All 115,917 compounds are identified only by their most diagnostic peaks, presented in 136,141 different spectra to allow faster identification based on easily-recognizable signatures. Covering chemicals from the broadest possible range of types, this three-volume set is a high-utility reference for today''s lab.

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Book SynopsisThe last few years have seen an unprecedented drive toward the application of proteomics to resolving challenging biomedical and biochemical tasks. Separation techniques combined with modern mass spectrometry are playing a central role in this drive. This book discusses the increasingly important role of mass spectrometry in proteomic research, and emphasizes recent advances in the existing technology and describes the advantages and pitfalls as well. * Provides a scientifically valid method for analyzing the approximatey 500,000 proteins that are encoded in the human genome * Explains the hows and whys of using mass spectrometry in proteomic analysis * Brings together the latest approaches combining separation techniques and mass spectrometry and their application in proteome analysis * Comments on future challenges and how they may be addressed * Includes sections on troubleshootingTrade Review"I highly recommend this book for anyone planning to get involved in proteomics technology or for one who is already involved…it provides an entertaining insight on the field..." (Microbe, March 2006) "...a must reference for anyone interested in proteomics. For me, if Proteomics Today is not in my backpack it will be within arms reach as a great reference to have on hand as I plan future experiments." (Journal of the American Society for Mass Spectrometry, January 2006) "…the book is highly recommended to all scientists interested in protein separation science, and well-thumbed copies will certainly be present in every self-respecting proteomic laboratory." (Proteomics, July 2005) ‘This book is well written and thus easy to read. It contains valuable information and extensive references for readers from a variety of backgrounds.’ (Analytical and Bioanalytical Chemistry, 12 January 2007) "…well-written and thus easy to read. It contains valuable information and extensive references for readers from a variety of backgrounds." (Analytical and Bioanalytical Chemistry, January 2007) Table of ContentsPREFACE TO PART I. ACKNOWLEDGMENT. I: INTRODUCTION TO PART I. 1. INSTRUMENTATION AND DEVELOPMENTS. 1.1 Introduction. 1.2 Ionization Techniques for Macromolecules. 1.3 Examples on Analytical Solutions Based on FAB–MS. 1.4 Electrospray Ionization. 1.5 Matrix-Assisted Laser Desorption Ionization. 1.6 Ion Detection. 1.7 Types of Analyzers. 1.8 Hybrid Analyzers. 1.9 Tandem Mass Spectrometry. 1.10 Current MS Instrumentation in Proteome Analyses. 1.11 Current MS-Based Proteomics. 1.12 Recent Achievements and Future Challenges. 1.13 Concluding Remarks. References. 2. PROTEOMICS IN CANCER RESEARCH. 2.1 Introduction. 2.2 Pancreatic Ductal Adenocarcinoma. 2.3 Proteomic Analysis of Human Breast Carcinoma. 2.4 Proteomic Profiling of Chemoresistant Cancer Cells. 2.5 Signal Pathway Profiling of Prostate Cancer. 2.6 Emerging Role of Functional and Activity-Based Proteomics in Disease Understanding. 2.7 Activity-Based Protein Profiling. 2.8 Probing Protein Functions Using Chromophore-Assisted Laser Inactivation. 2.9 Role of Protein–Tyrosine Kinases. 2.10 Concluding Remarks and Future Prospects. References. 3. CURRENT STRATEGIES FOR PROTEIN QUANTIFICATION. 3.1 Introduction. 3.2 Global Internal Standard Technology. 3.3 Differential In-Gel Electrophoresis. 3.4 Quantification of Modified Proteins. 3.5 Comments and Considerations. 3.6 Other Approaches. 3.7 Emerging Role of Microfluidic Devices. 3.8 Concluding Remarks. References. II: PROTEOMICS TODAY: SEPARATION SCIENCE AT WORK. 4. CONVENTIONAL ISOELECTRIC FOCUSING IN GEL MATRICES AND CAPILLARIES AND IMMOBILIZED pH GRADIENTS. 4.1 Introduction. 4.2 Conventional Isoelectric Focusing in Amphoteric Buffers. 4.3 Immobilized pH Gradients. 4.4 Capillary Isoelectric Focusing. 4.5 Separation of Peptides and Proteins by CZE in Isoelectric Buffers. 4.6 Conclusions. References. 5. SODIUM DODECYL SULFATE–POLYACRYLAMIDE GEL ELECTROPHORESIS. 5.1 Introduction. 5.2 SDS–Protein Complexes: a Refinement of the Model. 5.3 Theoretical Background of Mr Measurement by SDS–PAGE. 5.4 Methodology. 5.5 Gel Casting and Buffer Systems. 5.6 Blotting Procedures. 5.7 Conclusions. References. 6. TWO-DIMENSIONAL MAPS. 6.1 Introduction. 6.2 Some Basic Methodology Pertaining to 2D PAGE. 6.3 Prefractionation Tools in Proteome Analysis. 6.4 Multidimensional Chromatography Coupled to MS. 6.5 Protein Chips and Microarrays. 6.6 Nondenaturing Protein Maps. 6.7 Spot Matching in 2D Gels via Commercial Software. 6.8 Conclusions. References. INDEX.

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Book SynopsisState-of-the-art tools and applicationsfor food safety and food science research Atomic spectroscopy and mass spectrometry are important tools for identifying and quantifying trace elements in food products-elements that may be potentially beneficial or potentially toxic. The Determination of Chemical Elements in Food: Applications for Atomic and Mass Spectrometry teaches the reader how to use these advanced technologies for food analysis. With chapters written by internationally renowned scientists, it provides a detailed overview of progress in the field and the latest innovations in instrumentation and techniques, covering: Fundamentals and method development, selected applications, and speciation analysis Applications of atomic absorption spectrometry, inductively coupled plasma atomic emission spectrometry, and inductively coupled plasma mass spectrometry Applications to foods of animal origin and applications to foods of vegetable Table of ContentsPreface. Contributors. SECTION 1: FUNDAMENTALS AND METHOD DEVELOPMENT. 1. Improvement in Pretreatment and Analysis with Spectrometric Methods: A Typical Application to Routine Analysis.(K. Boutakhrit, F. Bolle, J.M. Degroodt, and L. Goeyens) 2. Solubilization: Trends of Development in Analytical Atomic Spectrometry for Elemental Food Analysis. (Henryk Matusiewicz) 3. Chemical Elements in Food and the Role of Atomic and Mass Spectrometry. Advantages and Drawbacks of the Determination of Selected Trace Elements in Foodstuffs by Atomic Absorption Spectrometry. (Lars Jorhem and Joakim Engman) 4. High-Resolution Continuum Source AAs and its Application to Food Analysis. (Bernhard Welz, Daniel L. G. Borges, and Uwe Heitmann) 5. Determining the Geographical Origin of Foods: Considerations when Designing Experimental Protocols and Choosing Analytical Approaches. (John Lewis and Simon Hird) 6. Methods Validation for Food Analysis: Concepts and Use of Statistical Techniques. (Joris Van Loco) 7. Demonstration of Measurement Capabilities by Means of Interlaboratory Comparison Schemes for Trace Element Analysis in Food. (Yetunde Aregbe, Piotr Robouch, and Thomas Prohaska) SECTION 2: SELECTED APPLICATIONS. 8. Applications of Inductively Coupled Plasma Mass Spectrometry to Trace Element research and Control. (Francesco Cubadda) 9. Danish Monitoring System for Foods 1998-2003. Content of As, Cd, Hg, Ni, Pb, and Se and Dietary Inake by Children and Adults. (Erik H. Larsen, Inge Rokkjar, and Tue Christensen) 10. Trace Elements in the Total Diet Typical of Northern Italy. (M. Bettinelli, S. Spezia, A. Gatti, A. Ronchi, C. Minoia, C. Roggi, and G. Turconi) 11. Car Catalytic Converters and the Contamination of Food by Platinum-Group Elements. (Chiara Frazzoli, Roberta Cammarone, and Sergio Caroli) 12. Arsenic and Other Potentially Toxic Trace Elements in Rice. (Chiara Frazzoli, Marilena D'Amato, Sergio Caroli, and Gyula Zaray) 13. Total Analysis and Distribution of Trace Elements in Human, Cow, and Formula Milk. (Rafael R. de la Flor St. Remy, Maria Luisa Fernandez Sanchez, and Alfredo Sanz-Medel) 14. Use of Spectrochemical Methods for the Determination of Metals in Fish and Other Seafood in Louisiana. (Joseph Sneddon) 15. Essential and Potentially Toxic Chemical Elements in Beverages. (Patricia Smichowksi and Daniel A. Batistoni) SECTION 3: SPECIATION ANALYSIS. 16. Species-Specific Determination of Metal(loid)-containing Food Additive sand Contaminants by Chromatography with ICP-MS Detection. (A. Polatajko, B. Bouyssiere, and J.Szpunar) 17. Elemental Speciation in Human Milk and Substitute Food for Newborns. (bernahrd Michalke, Maria Luisa Fernancez Sanchez, and Alfredo Sanz-Medel) 18. Measurement of Total Arsenic and Arsenic Species in Seafood By Q ICP-MS. (William A. Maher, Jason Kiry, and Frank Krikowa) 19. Sample Preparation Prior to As- and Se-Speciation. (Mihaly Dernovics and Peter Fodor) 20. Measurement of Total Se and Se Species in Seafood by Quadrupole Inductively Coupled Plasma Mass Spectrometry, Electrothermal Atomization Atomic Absorption Spectrometry, and High-Performance Liquid Chromatography Inductively Coupled Plasma Mass Spectrometry. (William A. Maher and Frank Kirkowa) 21. Application of ICP-MS for the Evaluation of Se Species in Food Related Products and in Dietary Supplements. (Katarzyna Wrobel, Kaximierz Wrobel, and Joseph A. Caruso) 22. Determination of Hg Species in Seafood. (Petra Krystek and Rob Ritsema) Author Index. Subject Index.

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Book SynopsisThe collection contains 2,979 EI mass spectra of androgens and estrogens and their trimethylsily-, O-methoxyoxime- and acetal derivatives. Each spectrum is accompanied by the structure and trivial name, molecular formula, molecular weight, nominal mass and base peak.

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