Spectrum analysis Books

Book SynopsisSpecialist Periodical Reports provide systematic and critical review coverage in major areas of chemical research. Compiled by teams of leading authorities in the relevant subject, the series creates a unique service for the active research chemist with regular critical in-depth accounts of progress in particular areas of chemistry. Subject coverage of all volumes is very similar and publication is on an annual or biennial basis. As EPR continues to find new applications in virtually all areas of modern science, including physics, chemistry, biology and materials science, this series caters not only for experts in the field, but also those wishing to gain a general overview of EPR applications in a given area.Table of ContentsPreface; Simulation of spectroscopic properties of Inorganic Compounds; Use of Synchrotron IR Radiation to study the Surface Chemistry of Inorganic Materials; Raman Spectroscopy of Graphene; Raman and IR spectroscopic studies on Fuel Cells; Spectroscopic and structural studies on Environmental Particles; Combined time-resolved SAXS and X-ray Spectroscopy methods; Solid state NMR of immobilised catalysts; Metal Coordinated Molecular Switches; NMR spectroscopy of supported organometallic catalysts; Nuclear Quadrupole Resonance Spectroscopy; Spectroscopy of metal dihydrogen and metal-hydride interactions.

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Book SynopsisThe aim of this title is to document the meeting exploring the key challenges in understanding the biological chemistry of metals. State of the art work using advanced physical and computational methods to probe the electronic structure and the reactivity at the active sites of metalloenzymes is discussed. These investigations are truly interdisciplinary and the development and application of physical methods and computational chemistry to biological problems require spectroscopists and theoretical chemists to collaborate with each other and with a wide range of other scientists, notably biochemists and coordination chemists. This is particularity true as spectroscopy and theory typically prove insight into slightly different aspects of reactivity. The book will provide substantial benefits to both experimentalists and theoreticians working in this filed.

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Book SynopsisIsotope Dilution Mass Spectrometry (IDMS) has become an essential tool in research laboratories and is increasingly used in routine analysis labs (including environmental, food safety and clinical applications). This is the first textbook to present a comprehensive and instructive view of the theory and applications of this growing technique. The main objective of this book is to cover the theory and applications of Isotope Dilution in Analytical Chemistry. The scope is comprehensive to include elemental analysis, speciation analysis, organic analysis and biochemical and clinical analysis together with applications in metabolism studies and traceability of goods. Until now there have been no books published with the same general scope (only book chapters on particular applications). This is a textbook focused at post-graduate level covering the basic knowledge required for doctoral studies in this field. Isotope Dilution Mass Spectrometry will also outline practical applications of interest for routine testing laboratories where isotope dilution procedures are implemented or can be implemented in the future. This unique book covers all the theoretical and practical aspects of Isotope Dilution Mass Spectrometry (IDMS). Due to the increasing application of IDMS in many research laboratories and the increasing implementation of IDMS methodologies in routine testing laboratories, scientists in industry and working in or affiliated to this area will this an invaluable source of information. Concerning the theoretical aspects, the authors present a uniform theoretical background which grows from previous developments in Organic, Speciation and Elemental analysis both in their own laboratory and in other laboratories around the world. This general approach will be simpler and will also include new emerging fields such as quantitative proteomics and metabolism studies.Trade ReviewThis book gives plenty of advice to both pure and applied chemists. This book provides helpful information on rarely considered aspects of isotope dilution. This book is the biggest vol- ume on isotope dilution mass spectrometry to date, and sci- entists of all abilities, whether beginners or experts, will be able to draw from this work. -- Juris Meija * Anal Bioanal Chem DOI 10.1007/s00216-014-7662-6 *Book’s topic Isotope dilution mass spectrometry (IDMS) has become a staple of analytical chemistry. One reason for this is that IDMS enables quantitation of an analyte without too much regard for incomplete extraction or digestion. Unlike the popular, related method of standard addition, which usually relies on extensive analytical response (peak area or signal intensity), isotope dilution uses intensive response: the isotope amount ratio. Although the principle behind isotope dilution is simple and can be explained using the analogy of catch-andrelease fish counting in a pond, the technical and theoretical details of implementing isotope dilution become complex rather quickly. Consequently, isotope dilution is not a onesize- fits-all panacea in analytical chemistry. This book tries to present many of the details that are important for accurate performance of isotope dilution. Contents This book consists of ten chapters. The introductory chapter provides an overview of isotope dilution mass spectrometry, including a brief historical outline of the method. The second chapter is devoted to the basic equations of IDMS, including double IDMS and exact-matching double IDMS. This chapter also provides the equations that extend the isotope dilution to more than two isotopes (that is, one isotope ratio). Chapter 3 discusses online IDMS, which allows isotope-dilution-based quantitation of multiple analytes containing the element of interest as they elute from the chromatographic column. This is a popular method in elemental speciation because it requires only one isotopic standard of an element, rather than one isotopic standard for each substance. Chapter 4 covers the topic on which the authors are recognized experts: the use of multiple isotopically labelled substances for quantitation of dynamic systems. This is the application for which isotope dilution offers the most substantial advantages over traditional methods. A popular example of this approach is the quantitation of Cr(VI) in the presence of Cr(III). It is possible for some of the Cr(III) to convert into Cr(VI) during sample preparation, and, to ascertain the amount of Cr(III) that was not originally present in the sample, one can add isotopic spikes of both Cr(III) and Cr(VI), each enriched in a different isotope of chromium. Chapter 5 deals with the natural isotopic composition of elements and how to use it to calculate the natural isotopic composition of complex substances, and chapter 6 provides guidance on selecting the isotopic spike. Chapters 7 and 8 provide technical discourse on the measurement of isotope ratios in elemental or molecular mass spectrometry. Chapter 9 discusses the traceability of IDMS results, emphasising the function of purity estimations of natural standards. Lastly, chapter 10 provides guidance on the uncertainty evaluation of IDMS results. This chapter discusses different sources of uncertainty, offers guidance on how to minimize these, and provides mathematical tools for combining all individual uncertainty components to estimate the uncertainty of the final result. Comparison with the existing literature Isotope dilution mass spectrometry features as a chapter in virtually all modern analytical chemistry textbooks. However, it is rare to find an entire book devoted to this subject. The closest alternative to this book is the small paperback Guidelines for Achieving High Accuracy in Isotope Dilution Mass Spectrometry by Sargent, Harrington, and Harte, published in 2002 by the Royal Society of Chemistry. However, the scope of this book is much more exhaustive, reflecting the numerous recent developments in the field. Critical assessment This book gives plenty of advice to both pure and applied chemists. However, isotope dilution mass spectrometry has developed substantially over the last few decades, and it is increasingly difficult to cover all aspects of the method. Among the topics almost entirely omitted from this book is the blank correction. In addition: chapter 7 discusses mass-bias correction in mass spectrometry and the fact that most corrections rely on comparisons between the measured isotope ratios and the “theoretical” values provided byIUPAC. However, no further guidance is given as to how these “theoretical” values are obtained in the first place. The discourse on standard atomic weights is, at times, not well researched. For example, the authors voice the opinion that “atomic-weight intervals are useless not only for trade and commerce but also for Chemical Metrology”. Such a comment is unfortunate, because it does nothing to improve knowledge. More research by the authors on this topic would most certainly have benefited this book, and would mean readers would not be presented with freshman mistakes whereby atomic weights are expressed in g mol−1, or such comments as “the mol is the reference for the determination of the atomic weights” (the opposite is true; it is the atomic weights which serve as the reference to determine the mole). Summary This book provides helpful information on rarely considered aspects of isotope dilution. The authors thus effectively dispel the notion that isotope dilution is a simplemethod that will always provide accurate results. The few above shortcomings notwithstanding, this book is the biggest volume on isotope dilution mass spectrometry to date, and scientists of all abilities, whether beginners or experts, will be able to draw from this work. -- Juris Meija * Anal Bioanal Chem DOI 10.1007/s00216-014-7662-6 *Table of Contents1 Introduction to Isotope Dilution Mass Spectrometry (IDMS);2 IDMS Procedures and Calculation Methods; 3 Online Isotope Dilution Mass Spectrometry; 4 The Use of Multiple Enriched Isotopes for IDMS; 5 The Isotope Composition of Natural-Abundance Elements and Molecules; 6 Selection of Isotopically Enriched Elements and Isotopically Labelled Molecules; 7 The Measurement of the Isotope Composition of the Elements; 8 The Measurement of the Isotope Composition of Molecules by Mass Spectrometry; 9 Traceability in Isotope Dilution Mass Spectrometry; 10 Uncertainty Evaluation in IDMS; Appendix Definition and Explanation of Symbols Used; Subject Index

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Book SynopsisThis book was triggered by the success story of sector field mass spectrometry in elemental and isotopic analysis since the first presentation of the mass spectrum of Ne a hundred years ago. The outstanding and unique features of sector field mass spectrometry - high sensitivity, high mass resolution and simultaneous multiple ion detection – have paved the way for its widespread and successful application across different scientific disciplines.　 Written, compiled and edited by world renowned experts, this book is intended to provide deep insight into the topic along with fundamental knowledge about elemental and isotopic analysis. Aimed at scientists in the field of natural and life sciences, instrument manufacturers, practitioners and graduate students, it provides solid information about the methodological background and analytical capabilities of sector field mass spectrometry. A detailed description of peculiarities and an overview of the most relevant applications making use of specific techniques employing sector field mass analysers (ICP-MS, GDMS, TIMS, SIMS and IRMS) are given, including a presentation of the currently available commercial instruments. This approach guarantees that readers are thoroughly introduced to and familiarized with the fascinating inter- and transdisciplinary field of sector field mass spectrometry.Table of ContentsIntroduction; History; Fundamentals; Analytical Instrumentation; Comparative Summary; Future development/Outlook; Subject Index

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Book SynopsisSpectroscopic Properties of Inorganic and Organometallic Compounds: Techniques, Materials and Applications provides a unique source of information in an important area of chemistry. Since Volume 40 the nature and ethos of this series have been altered to reflect a change of emphasis towards 'Techniques, Materials and Applications'. Researchers will now find up-to-date critical reviews which provide in-depth analyses of the leading papers in the field, with authors commenting of the quality and value of the work in a wider context. Focus areas will include structure-function relationships, photochemistry and spectroscopy of inorganic complexes, and catalysis; materials such as ceramics, cements, pigments, glasses and corrosion products; techniques such as advanced laser spectroscopy and theoretical methods.Table of ContentsPreface; IR spectroscopy of hydrides and its application to hydrogen bonding and proton transfer studies; Raman spectroscopy of graphene; Solid-state NMR: a key tool for the understanding at a molecular level of well-defined heterogeneous catalysts and surface chemistry on top of oxide materials; Raman spectroscopy for solid oxide fuel cells; Integrated analytical techniques for analysing individual environmental particles; Materials sciences using synchrotron infrared light sources; Metal-based molecular switches generated from dithienyl ethene (DTE); Nuclear quadrupole resonance spectroscopy; Simulation of spectroscopic properties of inorganic compounds; Combined time-resolved X-ray scattering and spectroscopy methods;Solid state NMR of immobilized catalysts and nanocatalysts

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Book SynopsisSpectroscopic Properties of Inorganic and Organometallic Compounds: Techniques, Materials and Applications provides a unique source of information in an important area of chemistry. Since Volume 40 the nature and ethos of this series have been altered to reflect a change of emphasis towards 'Techniques, Materials and Applications'. Researchers will now find up-to-date critical reviews which provide in-depth analyses of the leading papers in the field, with authors commenting of the quality and value of the work in a wider context. Focus areas will include structure-function relationships, photochemistry and spectroscopy of inorganic complexes, and catalysis; materials such as ceramics, cements, pigments, glasses and corrosion products; techniques such as advanced laser spectroscopy and theoretical methods.Table of ContentsElectrochemiluminesence of Ruthenium Complex and its Application in Biosensors; Spectroscopic Studies of Quantum Dots; Surface Enhanced IR Spectroscopy - Principles and Applications; NQR Spectroscopy; Raman Sensors for Inorganic Salt Solutions; Spectroscopic Studies of Metal Complexes

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Book SynopsisIntroducing astrochemistry to a wide audience, this book describes how molecules formed in chemical reactions occur in a range of environments in interstellar and circumstellar space, from shortly after the Big Bang up to the present epoch. Stressing that chemistry in these environments needs to be driven, it helps identify these drivers and the various chemical networks that operate giving rise to signature molecules that enable the physics of the region to be better understood. The book emphasises, in a non-mathematical way, the chemistry of the Milky Way Galaxy and its planet-forming regions, describes how other galaxies may have rather different chemistries and shows how chemistry was important even in the Early Universe when most of the elements had yet to be formed. This book will appeal to anyone with a general interest in chemistry, from students to professional scientists working in interdisciplinary areas and non-scientists fascinated by the evolving and exciting story of chemistry in the cosmos.Trade ReviewUK academics Williams (Univ. College London) and Hartquist (Univ. of Leeds) present an authoritative though skimpily documented account of the universe's evolution, from the prechemical times--shortly after the big bang--of isolated elementary particles and hyperenergetic photons, through the formation of atoms, to more complex molecules and dust particles, and finally to stars, planets, and galaxies. The emphasis is heavily chemical, with relatively brief focus on the physical dynamics of stellar fNmation and energy. The text is also unsparingly technical, though nonmathematical. The authors stipulate that the intended audienc;e is "anyone with a general interest in chemistry, from students to professional scientists." However, students will need a good background in chemistry and physics to follow the text. The presentation is adorned with stl'ikingly good color illustrations of deep-space objects in the throes of processes described. Unfortunately, bibliographic aids are limited to brief "Fwiher Reading" lists, dominated by the authors' and their students' contributions. The relatively terse index largely references individual scientists. There is no discussion (perhaps wisely; no one really understands it) ofthe "dark matter" and "dark energy" that may or may not, depending on cosmologists, dominate the evolution of galaxies and the universe. Js there a "dark chemistry"? Summing Up: Recommended. With reservations. Upper-division undergraduates through professionals. -- T R. Blackburn, former(v, American Chemical Society Petroleum Research Fund -- T R. Blackburn * CHOICE - Vol. 51 No. 08 *Table of ContentsIntroduction to Astrochemistry; Interstellar Molecular Hydrogen; Chemical Routes to Interstellar Molecules; Molecules in the Milky Way Galaxy; The Path to Planets; A Universe of Galaxies; The Early Universe; Why Chemistry is Important for Astronomy; Why Astronomy is Important for Chemistry; Subject Index

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Book SynopsisIn the rapidly growing field of metabolomics, a comprehensive book describing the state of the art in the application of NMR spectroscopy will be a key title for practitioners. Providing a unique resource of background knowledge, resources, instrumental platforms and software, this book will introduce relevant theory to the researcher as well as serve as a practical guide detailing key experiments and data handling procedures. Information available on common sample types will be described together with reference to the latest web-based resources available. Application-specific considerations will be discussed for a wide range of research topics. Written by an expert team as a service to the metabolomics community, this book will appeal to NMR spectroscopists, analytical chemists and biochemists especially those with an interest in medical applications.Table of ContentsInstrumental Platforms for NMR-based Metabolomics; NMR Pulse Sequences for Metabolomics; NMR Spectroscopy of Urine; NMR Spectroscopy of Serum and Plasma; High-resolution Magic-angle Spinning (HR-MAS) NMR Spectroscopy; Investigation of Tumor Metabolism by High-resolution Magic-angle Spinning (HR-MAS) Magnetic Resonance Spectroscopy (MRS); NMR in Environmental and Nutritional Research; NMR Foodomics; NMR-based Metabolomics: Understanding Plant Chemistry and Identification of Biologically Active Compounds; 1H NMR-based Metabolic Profiling in Infectious Disease Research; Imaging Metabolic Processes in Living Systems with Hyperpolarised 13C Magnetic Resonance; Advances in Computational Analysis of Metabolomic NMR Data; NMR Spectroscopy of Cell Culture, Tissues, and Other Biofluids

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Book SynopsisAs a component of post-genome science, the field of proteomics has assumed great prominence in recent years. Whereas quantitative analyses focussed initially on relative quantification, a greater emphasis is now placed on absolute quantification and consideration of proteome dynamics. Coverage of the topic of quantitative proteomics requires consideration both of the analytical fundamentals of quantitative mass spectrometry and the specific demands of the problem being addressed. Quantitative Proteomics aims to outline the state of the art in mass spectrometry-based quantitative proteomics, describing recent advances and current limitations in the instrumentation used, together with the various methods employed for generating high quality data. Details on both strategies describing how stable isotope labelling can be applied and methods for performing quantitative analysis of proteins in a label-free manner are given. The utility of these strategies to understanding cellular protein dynamics are then exemplified with chapters looking at spatial proteomics, dynamics of protein function as determined by quantifying changes in protein post-translational modification and protein turnover. Finally, a key application of these techniques to biomarker discovery and validation is presented, together with the rapidly developing area of quantitative analysis of protein-based foodstuffs. This exemplary book is essential reading for analytical and biological mass spectrometrists working in proteomics research, as well as those undertaking either fundamental or clinical-based investigations with an interest in understanding protein dynamics and/or biomarker assessment.Trade Review"Quantitative Proteomics should not be regarded only as an updated reference book of cutting-edge bottom-up strategies for quantitative proteomics. Its reading makes us reflect on the enormous experimental progress made possible by the recent developments magnificently summarized in the 15 chapters in this new volume of the series New Developments in Mass Spectrometry." -- Juan J. Calvete * Journal of Proteomics, Volume 108, 2014, Pages 494-496 *Bio-molecular cycles are to say the least exceedingly complex. Although many cycles have already been defined, relatively little is known about the macromolecular workhorses that are embedded in the cells that actually do the work. It is only in the last two decades, with major advances in instrumentation, that insights into these complex mechanisms have been possible. Analysing a moving target is difficult at any time. When that target is the determination of protein composition as a function of the cell cycle, its age and its response to extracellular stimuli, the process becomes one of taking a snapshot in time. By definition this monitors the quantitative changes taking place over time and mass spectrometry is one of very few techniques capable of achieving this objective. Even with this very powerful tool, a very careful selection of appropriate strategies is called for, and this book describes those that have achieved at least a degree of success. The greatest limitation is that quantitative proteomics relies on the use of peptide surrogates as read-outs for the actual protein amount. Such simulations are not always reliable, a major fact recognised and emphasised throughout all chapters. With this in mind the editors have assembled authors with the necessary knowledge combined with an ability to explain current practices whilst simultaneously stating the limitations. Most authors also propose new ideas and possible extensions that may well apply in the future. The book is divided into a description of the technology (two chapters); label-based protein quantification (three chapters); label-free protein quantification (three chapters); dynamic protein quantification (four chapters); and application of quantitative proteomics (three chapters). The division between labelled and label-free quantification is most useful. It allows for a rapid comparison between methods and easier selection of the most appropriate method. The challenge in any method is to determine the absolute protein quantification at any given time and then reproduce it. At the forefront of current methods are HPLC and electrospray MS. As always with this technology, a major issue is how to identify the most appropriate sample preparation method, an issue recognised by most authors. The most intriguing chapters are the last two. It is encouraging to see a chapter on blood plasma. The blood processing industry is a key to human survival, is a massively important industry, and yet receives relatively little publicity. It is in effect largely hidden from public view. Non-communicable diseases account for 60 % of the world’s fatalities, and yet many could be detected by biomarkers if the technology were available—and quantitative proteomics offers the promise of inexpensive automated procedures on the millions of samples of blood taken daily. Similarly, in the chapter on food, application of similar methods offers the prospect of determining allergies in food, the new plague of allergic reaction now suffered by some 30 % of the western populace. It is regrettable that this book is unlikely to be read by those responsible for allocation of research funding. Development of the described technology holds significant promise in delivering automated methods capable of early detection and therefore easier and cheaper treatment of many diseases. -- K. Jones, Chromatographia * Chromatographia (2015) 78:141–142 *"the editors have assembled authors with the necessary knowledge combined with an ability to explain current practices whilst simultaneously stating the limitations. Most authors also propose new ideas and possible extensions that may well apply in the future." -- K. Jones * Chromatographia (2015) 78:141–142 *Table of ContentsPractical Considerations and Current Limitations in Quantitative Mass Spectrometry-Based Proteomics; Targeted Proteomics Based on High Resolution Accurate Mass Spectrometry Measurement; Making Sense Out of the Proteome: The Utility of iTRAQ and TMT; Getting Absolute: Determining Absolute Protein Quantities via Selected Reaction Monitoring Mass Spectrometry; Proteomics Standards with Controllable Trueness - Absolute Quantification of Peptides, Phosphopeptides and Proteins Using ICP- and ESI-MS Label-Free Strategies for Protein Quantification; Overview and Implementation of Mass Spectrometry-Based Label-Free Quantitative Proteomics; MS1 Label-Free Quantification Using Ion Intensity Chromatograms in Skyline (Research and Clinical Applications); Label-Free Quantification of Proteins Using Data-Independent Acquisition; Spatial Proteomics: Practical Considerations for Data Acquisition and Analysis in Protein Subcellular Localisation Studies; Quantitative Analyses of Phosphotyrosine Cellular Signalling in Disease; Next Generation Proteomics: PTMs in Space and Time; Experimental and Analytical Approaches to Quantification of Protein Turnover on a Proteome-Wide Scale; Protein Quantification by MRM for Biomarker Validation; MRM-based Protein Quantification with Labelled Standards for Biomarker Discovery, Verification, and Validation in Human Plasma; Mass Spectrometry-Based Quantification of Proteins and Peptides in Food; Subject Index

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Book SynopsisThe emerging field of lipidomics has been made possible because of advances in mass spectrometry, and in particular tandem mass spectrometry of lipid ions generated by electrospray ionization. The ability to carry out basic biochemical studies of lipids using electrospray ionization is predicated upon understanding the behaviour of lipid derived ions following collision induced decomposition and mechanisms of product ion formation. During the past 20 years, a wealth of information has been generated about lipid molecules that are now analysed by mass spectrometry, however there is no central source where one can obtain basic information about how these very diverse biomolecules behave following collisional activation. This book brings together, in one volume, this information so that investigators considering using tandem mass spectrometry to structurally characterize lipids or to quantitate their occurrence in a biological matrix, will have a convenient source to review mechanism of decomposition reactions related to the diversity of lipid structures. A separate chapter is devoted to each of seven major lipid classes including fatty acids, eicosanoids and bioactive lipid mediators, fatty acyl esters and amides, glycerol esters, glycerophospholipids, sphingolipids, and steroids. Mechanistic details are provided for understanding the pathways of formation of major product ions and ions used for structural characterization. In most cases specific ancillary information has been critical to understand the pathways, including isotope labeling and high resolution analysis of precursor and product ions. For a few specific examples such data is missing and pathways are proposed as a means to initiate further mass spectral experiments to prove or disprove pathway hypotheses. While this work largely centres on the lipid biochemistry of animal (mammalian) systems, general principles can be taken from the specific examples and applied to lipid biochemistry found in plants, fungi, prokaryotes and archeal organisms.Table of ContentsIntroduction; Fatty Acids; Bioactive Lipid Mediators; Glycerolipids; Glycerolphospholipids; Sphingolipids; Sterol Lipids; Index

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Book SynopsisAmbient ionization has emerged as one of the hottest and fastest growing topics in mass spectrometry enabling sample analysis with minimal sample preparation. Introducing the subject and explaining the basic concepts and terminology, this book will provide a comprehensive, unique treatise devoted to the subject. Written by acknowledged experts, there are full descriptions on how new ionization techniques work, with an overview of their strengths, weaknesses and applications. This title will bring the reader right up to date, with both applications and theory, and will be suitable as a tutorial text for those starting in the field from a variety of disciplines.Trade Review"fulfils the need to collate all the current knowledge about this rapidly evolving field." "this book will be an invaluable reference for anybody working in this field from undergraduates through to experienced mass spectrometrists." -- Andrew Ray * Published in Chromatographia *Table of ContentsAn Introduction to Ambient Ionization Mass Spectrometry; Direct Analysis in real time (DART®); Ionization Mechanisms of Direct Analysis in Real Time (DART); Atmospheric Samples Analysis Probe (ASAP) Mass Spectrometry; Ambient Analysis by Thermal Desorption Atmospheric Pressure Photoionization; Low Temperature Plasma Probe; Flowing Atmospheric Pressure Afterglow (FAPA), the Plasma-based Source for your ADI-MS needs; Spray Desorption Collection and DESI Mechanisms; Easy Ambient Sonic-Spray Ionization; Secondary Electrospray Ionization; Probe Electrospray Ionization; Desorption Electrospray Mass Spectrometry; Surface Acoustic Wave Nebulization; Laser Ablation Electrospray Ionization Mass Spectrometry: Mechanisms, Configurations and Imaging Applications; Electrospray Laser Desorption Ionization Mass Spectrometry; Paper Spray; Inlet and Vacuum Ionization from Ambient Conditions; Enabling Automated Sample Analysis by Direct Analysis in Real Time (DART) Mass Spectrometry; Laser Ablation Electrospray Ionization Mass Spectrometry (LAESI®-MS): Ambient Ionization Technology for 2D and 3D Molecular Imaging; Liquid Extraction Surface Analysis Mass Spectrometry (LESA MS): Combining Liquid Extraction, Surface Profiling and Ambient Ionization Mass Spectrometry in One Novel Analysis Technique; Subject Index

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Book SynopsisThis volume explores the use of mass spectrometry for biomedical applications. Chapters focus on specific therapeutic areas such as oncology, infectious disease, and psychiatry. Additional chapters focus on methodology, technologies and instrumentation, as well as on analysis of protein-protein interactions, protein quantitation, and protein post-translational modifications. Various omics fields such as proteomics, metabolomics, glycomics, lipidomics, and adductomics are also covered. Applications of mass spectrometry in biotechnological and pharmaceutical industry are also discussed. This volume provides readers with a comprehensive and informative manual that will allow them to appreciate mass spectrometry and proteomic research, but also to initiate and improve their own work. This book acts as a technical guide as well as a conceptual guide to the newest information in this exciting field.Table of Contents1. Mass Spectrometry for Proteomics-based Investigation2. MALDI profiling and applications in medicine3. Applications of Matrix-Assisted Laser Desorption Ionization In-Source Decay Mass Spectrometry4. Proteome imaging: from classic to modern mass spectrometry-based molecular histology5. Mass Spectrometry-Based Tissue Imaging of Small Molecules6. Sequencing Proteins from Bottom to Top: Combining Techniques for Full Sequence Analysis of Glucokinase7. Proteomics and non-proteomics approaches to study stable and transient protein-protein interactions8. Contribution of Mass spectrometry-based Proteomics to Discoveries in Developmental Biology9. Profiling optimal conditions for capturing EDEM proteins complexes in melanoma using mass spectrometry10. The Methods employed in Mass Spectrometric Analysis of Posttranslational Modifications (PTMs) and Protein–Protein Interactions (PPIs)11. Identification of post-translational modifications (PTMs) of proteins by mass spectrometry12. Sequence Variant and Post-translational Modification Analysis During Cell Line Selection via High-throughput Peptide Mapping13. Selective derivatization of hexahistidine-tagged recombinant proteins14. Investigation of Antibody-Drug Conjugates by Mass Spectrometry15. Mass Spectrometry- and Computational Structural Biology-Based Investigation of Proteins and Peptides16. Strategies for Membrane Protein Analysis by Mass Spectrometry17. The Potential for Ion Mobility in Pharmaceutical and Clinical Analyses18. Application of Ion Mobility Mass Spectrometry in Lipidomics19. Mass Spectrometry in Advancement of Redox Precision Medicine20. Applications for mass spectrometry in the study of ion channel structure and function21. Immuno – affinity Mass Spectrometry: A Novel Approaches with Biomedical Relevance22. Developing well-annotated species-specific protein databases using comparative proteogenomics23. Stoichiometry of heavy metal binding to peptides involved in Alzheimer’s disease: mass spectrometric evidence24. Role of mass spectrometry in investigating a novel protein: the example of Tumor Differentiation Factor (TDF)25. Mass Spectrometry-Based Biomarkers in Drug Developmen26. Combinatorial Electrophoresis and Mass Spectrometry-Based Proteomics in Breast Milk for Breast Cancer Biomarker Discovery27. Proteomic approaches to dissect neuronal signalling pathways28. Mass Spectrometry for the Study of Autism and Neurodevelopmental Disorders29. Simplifying the proteome: Analytical strategies for improving peak capacity30. Exploration of nicotine metabolism in Paenarthrobacter nicotinovorans pAO1 by microbial proteomics31. Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) for Quantitative Proteomics32. Mass spectrometry based comparative proteomics using one dimensional and two dimensional SDS-PAGE of rat atria induced with obstructive sleep apnea33. 2D SDS PAGE in combination with western blotting and mass spectrometry is a robust method for protein analysis with many applications.34. Pulse SILAC approaches to the measurement of cellular dynamics35. Protein Biomarkers in Major Depressive Disorder: an Update36. A Pilot Exploratory Proteomics Investigation of Mental Fatigue and Mental Energy37. Metabolomics and biomarker discovery38. Analytical Methods for Mass Spectrometry-Based Metabolomics Studies39. Trends in analysis of cortisol and its derivatives40. Detection of biomedically relevant stilbenes from wines by mass spectrometry41. Mass spectrometry as a complementary approach for noncovalently bound complexes based on cyclodextrins42. Trends in glycolipid biomarker discovery in neurodegenerative disorders by mass spectrometry43. Non-targeted Screening in Environmental Monitoring Programs44. Mass Spectrometric DNA Adduct Quantification by Multiple Reaction Monitoring and its Future Use for the Molecular Epidemiology of Cancer45. Bottlenecks in proteomics: an update46. Recent Applications of Mass Spectrometry at Clarkson University Index

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Book SynopsisThis open access book, edited and authored by a team of world-leading researchers, provides a broad overview of advanced photonic methods for nanoscale visualization, as well as describing a range of fascinating in-depth studies. Introductory chapters cover the most relevant physics and basic methods that young researchers need to master in order to work effectively in the field of nanoscale photonic imaging, from physical first principles, to instrumentation, to mathematical foundations of imaging and data analysis. Subsequent chapters demonstrate how these cutting edge methods are applied to a variety of systems, including complex fluids and biomolecular systems, for visualizing their structure and dynamics, in space and on timescales extending over many orders of magnitude down to the femtosecond range. Progress in nanoscale photonic imaging in Göttingen has been the sum total of more than a decade of work by a wide range of scientists and mathematicians across disciplines, working together in a vibrant collaboration of a kind rarely matched. This volume presents the highlights of their research achievements and serves as a record of the unique and remarkable constellation of contributors, as well as looking ahead at the future prospects in this field. It will serve not only as a useful reference for experienced researchers but also as a valuable point of entry for newcomers. Table of ContentsPart I: Fundamentals and Tutorials.- Basic Knowledge in STED Nanoscopy (A. Egner, C. Geisler, and R. Siegmund).- Basic Knowledge in Coherent X-ray Imaging (T. Salditt, A.-L. Robisch).- Basic Knowledge: X-ray Focusing & Optics (T. Salditt and M. Osterhoff).- Statistical Foundations of Nanoscale Photonic Imaging (A. Munk, T. Staudt, and F. Werner).- Inverse Problems (T. Hohage, B. Sprung, and F. Weidling).- Proximal Methods for Image Processing (D. R. Luke).- Part II: Progress and Perspectives.- Quantifying the Number of Molecules in STED/RESOLFT Nanoscopy (J. Keller-Findeisen, S. Sahl, and S. W. Hell).- Metal-Induced Energy Transfer Imaging (A. I. Chizhik, and J. Enderlein).- Reversibly Switchable Fluorescent Proteins for RESOLFT Nanoscopy (N. A. Jensen, I. Jansen, M. Kamper, and S. Jakobs).- A Statistical and Biophysical Toolbox to Elucidate Structure and Formation of Stress Fibers (B. Eltzner, L. Hauke, S. Huckemann, F. Fehfeldt, and C. Wollnik).- Photonic Imaging with Statistical Guarantees: From Multiscale Testing to Multiscale Estimation (A. Munk, K. Proksch, H. Li, and F. Werner).- Efficient, Quantitative Numerical Methods for Statistical Image Deconvolution and Denoising (D. R. Luke, C. Charitha, R. Shefi, and Y. Malitsky).- Holographic Imaging and Tomography of Biological Cells and Tissues (T. Salditt, and M. Töpperwien).- Constrained Reconstructions in X-ray Phase Contrast Imaging: Uniqueness, Stability and Algorithms (S. Maretzke, T. Hohage).- Scanning Small-Angle X-ray Scattering and Coherent X-ray Imaging of Cells (T. Salditt and S. Köster).- Single Particle Imaging with FEL using Photon Correlations (B. von Ardenne and H. Grubmüller).- Development of Ultrafast X-ray Free Electron Laser Tools in (Bio)Chemical Research (S. Techert, S. Thekku Veedu, S. Bari).- Polarization-sensitive Coherent Diffractive Imaging Using HHG (S. Zayko, O. Kfir, and C. Ropers).- Nonlinear Light Generation in Localized Fields Using Gases and Tailored Solids (M. Sivis and C. Ropers).- Wavefront and Coherence Characteristics of Extreme UV and Soft X-ray Sources (B. Schäfer, B. Flöter, T. Mey, and K. Mann).- Laboratory-scale Soft X-ray Source for Microscopy and Absorption Spectroscopy (M. Müller and K. Mann).- Multilayer Zone Plates for Hard X-ray Imaging (M. Osterhoff and H.-U. Krebs).- Convergence Analysis of Iteraive Algorithms for Phase Retrieval (D. R. Luke and A.-L. Martins).- One-Dimensional Discrete-Time Phase Retrieval (R. Beinert and G. Plonka).

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Book SynopsisWritten by three leading experts in the field, this textbook describes and explains all aspects of the scanning probe microscopy. Emphasis is placed on the experimental design and procedures required to optimize the performance of the various methods. Scanning Probe Microscopy covers not only the physical principles behind scanning probe microscopy but also questions of instrumental designs, basic features of the different imaging modes, and recurring artifacts. The intention is to provide a general textbook for all types of classes that address scanning probe microscopy. Third year undergraduates and beyond should be able to use it for self-study or as textbook to accompany a course on probe microscopy. Furthermore, it will be valuable as reference book in any scanning probe microscopy laboratory. Novel applications and the latest important results are also presented, and the book closes with a look at the future prospects of scanning probe microscopy, also discussing related techniques in nanoscience. Ideally suited as an introduction for graduate students, the book will also serve as a valuable reference for practising researchers developing and using scanning probe techniques.Table of ContentsIntroduction to Scanning Probe Microscopy.- Overview.- Basic Concepts.- Introduction to Scanning Tunneling Microscopy.- Tunneling: A Quantum-Mechanical Effect.- Instrumental Aspects.- Resolution Limits.- Observation of Confined Electrons.- Spin-Polarized Tunneling.- Observation of the Kondo Effect and Quantum Mirage.- Force Microscopy.- Concept and Instrumental Aspects.- Relevant Forces.- Operation Modes in Force Microscopy.- Contact Force Microscopy.- Dynamic Force Microscopy.- Tapping Mode Force Microscopy.- Further Modes of Force Microscopy.- Force Resolution and Thermal Noise.- High-speed AFM.- Multifrequency AFM.- MFM and Related Techniques.- MFM Operation Modes.- Contrast Formation.- Magnetic Resonance Force Microscopy.- Other Members of the SPM Family.- Artifacts in SPM.- Future Aspects of SPM.

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Book SynopsisThis textbook is designed for graduate students to introduce the basic concepts of Nuclear Magnetic Resonance spectroscopy (NMR), spectral analysis and modern developments such as multidimensional NMR, in reasonable detail and rigor. The book is self-contained, so, a unique textbook in that sense with end of chapter exercises included supported by a solution manual. Some of the advanced topics are included as Appendices for quick reference. Students of chemistry who have some exposure to mathematics and physics will benefit from this book and it will prepare them to pursue research in different branches of Chemistry or Biophysics or Structural Biology.​Table of ContentsChapter-1: BASIC CONCEPTS 1.1 Nuclear Spin and Magnetic Moments 1.2 Nuclear Spins in a Magnetic Field 1.3 Spin Lattice Relaxation 1.4 Spin temperature 1.5 Resonance Absorption of Energy and The NMR Experiment 1.5.1. The basic NMR spectrometer 1.6 Kinetics of Resonance Absorption 1.7 Selection Rules 1.8 Line widths 1.9 Bloch equations 1.10 More about relaxation 1.11 Sensitivity EXERCISES CHAPTER 2: HIGH RESOLUTION NMR SPECTRA OF MOLECULES 2.1 Introduction 2.2 Chemical Shift 2.2.1 Anisotropy of chemical shifts 2.2.2 Factors Influencing Isotropic Chemical shifts 2.3 Spin-Spin Coupling 2.4 Analysis of NMR spectra of molecules 2.4.1 First Order Analysis 2.4.2 Quantum Mechanical Analysis 2.5 Dynamic Effects in the NMR spectra 2.5.1 Two site Chemical Exchange 2.5.2. Collapse of spin multiplets 2.5.3 Conformational Averaging of J- values EXERCISES CHAPTER 3: FOURIER TRANSFORM NMR 3.1 Introduction 3.2 Principles of Fourier transform NMR 3.3 Theorems on Fourier transforms 3.4 The FTNMR Spectrometer 3.5. Practical aspects of recording FTNMR spectra 3.5.1. Carrier Frequency and off-set 3.5.2. RF pulse 3.5.3. Free Induction Decay (FID) and the spectrum 3.5.4. Single channel and quadrature detection 3.5.5. Signal digitization and sampling 3.5.6. Folding of signals 3.5.7. Acquisition time and the resolution 3.5.8. Signal averaging and Pulse repetition rate 3.6. Data processing in FT NMR 3.6.1. Zero filling 3.6.2. Digital filtration or window multiplication or apodization 3.7 Phase correction 3.8. Dynamic range in FTNMR 3.9. Spin-echo 3.10. Measurement of relaxation times 3.10.1. Measurement of relaxation time 3.10.2. Measurement of relaxation time 3.11. Water suppression through spin-echo: Watergate 3.12 Spin decoupling 3.13 Broad band decoupling 3.14 Biliniear Rotational Decoupling (BIRD) EXERCISES CHAPTER 4: POLARIZATION TRANSFER 4.1 Introduction 4.2 Experimental Schemes 4.3 Origin of NOE 4.3.1 A simplified treatment 4.3.2 A more rigorous treatment 4.4 Steady state NOE 4.5 Transient NOE 4.6. Selective population inversion 4.7. INEPT 4.7.1. Disadvantages of INEPT 4.8 Refocused INEPT 4.9 DEPT EXERCISES CHAPTER 5: Density matrix description of NMR 5.1 Introduction 5.2 Density matrix 5.3 Elements of Density Matrix 5.4. Time evolution of density operator 5.5. Matrix representations of RF pulses 5.6. Product Operator Formalism 5.6.1. Basis operator sets 5.6.2. Time-evolution of Cartesian Basis Operators 5.6.2.1 Free evolution under the influence of the Hamiltonian 5.6.2.2 Chemical Shift evolution 5.6.2.3 Scalar coupling evolution 5.6.2.4 Rotation by pulses 5.6.2.5 Calculation of the spectrum of J-coupled two spin system EXERCISES Chapter 6: Multidimensional NMR Spectroscopy 6.1 Segmentation of the time axis 6.2 Two dimensional NMR 6.3 Two-dimensional Fourier Transformation in NMR 6.4 Peak shapes in 2D spectrum 6.5 Quadrature detection in two-dimensional NMR 6.6 Types of 2D-NMR spectra 6.6.1 2D- resolution/ separation experiments 6.6.2. Two-dimensional correlation experiments 6.6.2.1 The COSY experiment 6.6.2.1.1 COSY of two-spins 6.6.2.1.2 COSY of three-spins 6.6.2.1.3 Disadvantages of COSY 6.6.2.2 Double-Quantum Filtered COSY (DQF-COSY) 6.6.2.3 Total Correlation Spectroscopy (TOCSY) 6.6.2.4 Two-dimensional Nuclear Overhauser Effect spectroscopy (2D-NOESY) 6.6.2.5 Two-dimensional ROESY 6.6.3 Two-dimensional heteronuclear correlation experiments 6.6.3.1 Heteronuclear COSY 6.6.3.2 Heteronuclear Multiple Bond Correlation (HMBC) 6.6.3.3 Combination of mixing sequences 6.7 Three dimensional NMR 6.7.1 The CT-HNCA experiment 6.7.2 The HNN experiment 6.7.3 The constant-time HN(CO)CA experiment 6.7.4 The HN(C)N experiment EXERCISES APPENDIX A1. Hamiltonian of dipole-dipole interaction A2. Chemical Shift Anisotropy A3. Solid state NMR: basic features A4. Coherence selection by linear Field Gradients A5. Pure shift NMR: ZS and PSYCHE methods A6. HADAMARD NMR for selective excitation

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Book SynopsisThis book reviews the latest advances in mass spectrometry (MS) techniques applied to food safety and environment quality, and it discusses the recent improvements in sample preparation and MS platforms for screening of emerging contaminants. Expert contributors discuss the current applications from omics to the screening of emerging contaminants and nanomaterials in food and environmental matrices, and particular attention is given to the opportunities that MS offers for guarantying food security and promoting the sustainable use of ecosystems. Divided into 13 chapters, the book covers topics such as the handling and preparation of food and environmental samples for MS, foodomics, environmental omics, ambient ionization techniques in food and environmental chemistry, and chip-based separation devices coupled to MS. Readers will also find a comprehensive overview of several MS techniques applied to food and environmental chemistry, including elemental, isotopic, chiral, ion mobility, chromatographic and imaging MS. This book will appeal not only to students and researchers, but also to professionals working with MS platforms in food safety and environmental quality. The different advances and promising applications described in this work will be of paramount importance for ensuring food safety and environment health for current and future generations.Table of ContentsAn Overview of the state-of-the-art: Mass Spectrometry in Food and Environment.- Food and environmental samples handling and preparation for mass spectrometry.- Elemental Mass Spectrometry in food and environmental chemistry.- Isotopic mass spectrometry in food and environmental chemistry.- Chromatographic –mass spectrometry based screening methods in food and environmental chemistry.- Chromatographic-high resolution mass spectrometry in food and environmental chemistry.- Omics approaches (metabolomics, lipidomics, proteomics, foodomics, environmentalomics).- Thermal desorption and pyrolysis combined with gas chromatography mass spectrometry in food and environmental chemistry.- Chiral Mass spectrometry in food and environmental chemistry.- Ambient Ionization Techniques in food and environmental chemistry.- Ion Mobility Mass Spectrometry in food and environmental chemistry.- Imaging mass spectrometry in food and environmental chemistry.- Chip-based separation devices coupled to mass spectrometry in food and environmental chemistry.

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Book Synopsis

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Book Synopsis

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Book Synopsis

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Book Synopsis

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Book Synopsis

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Book Synopsis

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Book SynopsisThis fifth edition provides information on techniques needed to analyze foods for chemical and physical properties. The book is ideal for undergraduate courses in food analysis and is also an invaluable reference to professionals in the food industry. General information chapters on regulations, labeling, sampling, and data handling provide background information for chapters on specific methods to determine chemical composition and characteristics, physical properties, and objectionable matter and constituents. Methods of analysis covered include information on the basic principles, advantages, limitations, and applications. Sections on spectroscopy and chromatography along with chapters on techniques such as immunoassays, thermal analysis, and microscopy from the perspective of their use in food analysis have been expanded. Instructors who adopt the textbook can contact the editor for access to a website with related teaching materials.Table of ContentsIntroduction to Food Analysis.- United States Government Regulations and International Standards Related to Food Analysis.- Nutrition Labeling.- Evaluation of Analytical Data Sampling and Sample Preparation.- Basic Principles of Spectroscopy.- Ultraviolet, Visible, and Fluorescence Spectroscopy.- Infrared and Raman Spectroscopy.- Atomic Absorption Spectroscopy, Atomic Emission Spectroscopy, and Inductively Coupled Plasma-Mass Spectrometry.- Nuclear Magnetic Resonance.- Mass Spectrometry.- Basic Principles of Chromatography.- High Performance Liquid Chromatography.- Gas Chromatography.- Moisture and Total Solids Analysis.- Ash Analysis.- Fat Analysis.- Protein Analysis.- Carbohydrate Analysis.- Vitamin Analysis.- Traditional Methods for Mineral Analysis.- pH and Titratable Acidity.- Fat Characterization.- Protein Separation and Characterization Procedures.- Determination of (Total) Phenolics and Antioxidant Capacity in Food and Ingredients.- Application of Enzymes in Food Analysis.- Immunoassays.- Determination of Oxygen Demand.- Rheological Principles for Food Analysis.- Thermal Analysis.- Color Analysis.- Food Microstructure Techniques.- Analysis of Food Contaminants, Residues and Chemical Constituents of Concern.- Analysis for Extraneous Matter.- Food Forensic Investigation.

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Book SynopsisPreface. 1 Introduction. 2 Non-interacting Electrons.3 Electron-electron interaction.4 Phonons.5 Transport theory.6 Optical properties.7 Phase transitions.8 Low dimensional semiconductors.9 Shortcut of theoretical physics.

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Book SynopsisNuclear magnetic resonance (NMR) spectroscopy is one of the most powerful and widely used techniques in chemical research for investigating structures and dynamics of molecules. Advanced methods can even be utilized for structure determinations of biopolymers, for example proteins or nucleic acids. NMR is also used in medicine for magnetic resonance imaging (MRI). The method is based on spectral lines of different atomic nuclei that are excited when a strong magnetic field and a radiofrequency transmitter are applied. The method is very sensitive to the features of molecular structure because also the neighboring atoms influence the signals from individual nuclei and this is important for determining the 3D-structure of molecules. This new edition of the popular classic has a clear style and a highly practical, mostly non-mathematical approach. Many examples are taken from organic and organometallic chemistry, making this book an invaluable guide to undergraduate and graduate students of organic chemistry, biochemistry, spectroscopy or physical chemistry, and to researchers using this well-established and extremely important technique. Problems and solutions are included.Trade Review“Few good textbooks on NMR Spectroscopy are available at either the undergraduate or graduate levels. For those who want to go beyond elementary organic chemistry but without delving into all the mathematics Friebolin’s book is probably the best among this category.” (Journal of Chemical Education, 5 June 2014)Table of ContentsPREFACE INTRODUCTION Literature Units and Constants PART I: Basic Principles and Applications THE PHYSICAL BASIS OF THE NUCLEAR MAGNETIC RESONANCE EXPERIMENT The Quantum Mechanical Model for the Isolated Proton Classical Description of the NMR Experiment Experimental Verification of Quantized Angular Momentum and of the Resonance Equation The NMR Experiment on Compact Matter and the Principle of the NMR Spectrometer Magnetic Properties of Nuclei beyond the Proton THE PROTON MAGNETIC RESONANCE SPECTRA OF ORGANIC MOLECULES - CHEMICAL SHIFT AND SPIN - SPIN COUPLING The Chemical Shift Spin - Spin Coupling GENERAL EXPERIMENTAL ASPECTS OF NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY Sample Preparation and Sample Tubes Internal and External Standards; Solvent Effects Tuning the Spectrometer Increasing the Sensitivity Measurement of Spectra at Different Temperatures PROTON CHEMICAL SHIFTS AND SPIN - SPIN COUPLING CONSTANTS AS FUNCTIONS OF STRUCTURE Origin of Proton Chemical Shifts Proton - Proton Spin - Spin Coupling and Chemical Structure THE ANALYSIS OF HIGH-RESOLUTION NUCLEAR MAGNETIC RESONANCE SPECTRA Notation for Spin Systems Quantum Mechanical Formalism The Hamilton Operator for High-Resolution Nuclear Magnetic Resonance Spectroscopy Calculation of Individual Spin Systems THE INFLUENCE OF MOLECULAR SYMMETRY AND CHIRALITY ON PROTON MAGNETIC RESONANCE SPECTRA Spectral Types and Structural Isomerism Influence of Chirality on the NMR Spectrum Analysis of Degenerate Spin Systems by Means of 13C Satellites and H/D Substitution PART II: Advanced Methods and Applications THE PHYSICAL BASIS OF THE NUCLEAR MAGNETIC RESONANCE EXPERIMENT. The NMR Signal by Pulse Excitation Relaxation Effects Pulse Fourier-Transform (FT) NMR Spectroscopy Experimental Aspects of Pulse Fourier-Transform Spectroscopy Double Resonance Experiments TWO-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY Principles of Two-Dimensional NMR Spectroscopy The Spin Echo Experiment in Modern NMR Spectroscopy Homonuclear Two-Dimensional Spin Echo Spectroscopy: Separation of the Parameters J and d for Proton NMR Spectra The COSY Experiment - Two-Dimensional 1H,1H Shift Correlations The Product Operator Formalism Phase Cycles Gradient Enhanced Spectroscopy Universal Building Blocks for Pulse Sequences Homonuclear Shift Correlation by Double Quantum Selection of AX Systems - the 2D-INADEQUATE Experiment Single-Scan 2D NMR MORE 1D AND 2D NMR EXPERIMENTS: THE NUCLEAR OVERHAUSER EFFECT - POLARIZATION TRANSFER - SPIN LOCK EXPERIMENTS - 3D NMR The Overhauser Effect Polarization Transfer Experiments Rotating Frame Experiments Multidimensional NMR Experiments CARBON-13 NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY Historical Development and the Most Important Areas of Application Experimental Aspects of Carbon-13 Nuclear Magnetic Resonance Spectroscopy Carbon-13 Chemical Shifts Carbon-13 Spin - Spin Coupling Constants Carbon-13 Spin - Lattice Relaxation Rates SELECTED HETERONUCLEI Semimetals and Non-metals with the Exception of Hydrogen and Carbon Main Group Metals Transition Metals INFLUENCE OF DYNAMIC EFFECTS ON NUCLEAR MAGNETIC RESONANCE SPECTRA Exchange of Protons between Positions with Different Larmor Frequencies Internal Dynamics of Organic Molecules Intermolecular Exchange Processes Line Broadening by Fast Relaxing Neighboring Nuclei NUCLEAR MAGNETIC RESONANCE OF PARTIALLY ORIENTED MOLECULES AND SOLID STATE NMR Nuclear Magnetic Resonance of Partially Oriented Molecules High-Resolution Solid State Nuclear Magnetic Resonance Spectroscopy SELECTED TOPICS OF NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY Isotope Effects in Nuclear Magnetic Resonance Nuclear Magnetic Resonance Spectroscopy of Paramagnetic Materials Chemically Induced Dynamic Nuclear Polarization (CIDNP) Diffusion-Controlled Nuclear Magnetic Resonance Spectroscopy - DOSY Unconventional Methods for Sensitivity Enhancement - Hyperpolarization Nuclear Magnetic Resonance in Biochemistry and Medicine INDEX

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Book SynopsisDieses Lehrbuch bietet eine umfassende Einführung in die moderne chemische Labor-Analytik. Es führt in die theoretischen Grundlagen ein und stellt immer wieder die Bezüge zur Anwendung im Labor her. Die besondere Bedeutung der Analytik in Chemie-, Bio- und Umweltwissenschaften werden mit Nachdruck deutlich gemacht. In den Kapiteln fallen neben flüssig geschriebenen Texten und anschaulichen Graphiken vor allem Boxen mit interessanten Anwendungsbeispielen, kurzen Versuchsbeschreibungen, zusammenfassenden Abschnitten zur Rekapitulation des Gelernten und unzähligen Übungen mit teils ausführlichen, teils knappen Antworten auf. Alle modernen Techniken finden Erwähnung.Eine englischsprachige Internet-Seite ergänzt Tutorien, Arbeitsblätter und relevante Journals. Trade Review“... Neben grundlegenden Techniken behandelt das Buch auch moderne Analysemethoden auf dem neuesten Stand der Geräteentwicklung. Dabei gibt der Autor viel Hilfestellung zum Versuchsaufbau, sodass auch Doktoranden noch von dem Buch profitieren werden.” (in: PZ Pharmazeutische Zeitung, Heft 27, 2015)“... ist dieses Lehrbuch nicht nur Studierenden der Chemie, sondern auch ausgewählter Studiengänge aus den Bereichen Biowissenschaften, Laboratoriumsmedizin sowie Verfahrenstechnik sehr zu empfehlen.“ (Dr. Dieter Holzner, in: Chemie-leben-Biotechnik CLB, Jg. 65, Heft 9-10, 2014)Table of Contents0 Der analytische Prozess.- 1 Chemische Messungen.- 2 Handwerkszeug des Analytikers.- 3 Experimentelle Fehler.- 4 Statistik.- 5 Qualitätssicherung und Kalibrationsmethoden.- 6 Das chemische Gleichgewicht.- 7 Aktivität und systematische Behandlung von Gleichgewichten.- 8 Einprotonige Säure-Base-Gleichgewichte.- 9 Mehrprotonige Säure-Base-Gleichgewichte.- 10 Säure-Base-Titrationen.- 11 Komplexometrische Titrationen.- 12 Gleichgewichtsprobleme für Fortgeschrittene.- 13 Grundlagen der Elektrochemie.- 14 Elektroden und Potentiometrie.- 15 Redox-Titrationen.- 16 Elektroanalytische Methoden.- 17 Grundlagen der Spektralphotometrie.- 18 Anwendungen der Spektralphotometrie.- 19 Spektralphotometer.- 20 Atomspektroskopie.- 21 Massenspektrometrie.- 22 Einführung in Analytische Trennverfahren.- 23 Gaschromatographie.- 24 Hochleistungsflüssigkeitschromatographie.- 25 Chromatographische Methoden und Kapillarelektrophorese.- 26 Gravimetrische Analyse, Fällungstitrationen und Verbrennungsanalyse.- 27 Probenvorbereitung.

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