{"product_id":"analyzing-biomolecular-interactions-by-mass-spectrometry-9783527334643","title":"Analyzing Biomolecular Interactions by Mass Spectrometry","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003eThis monograph reviews all relevant technologies based on mass spectrometry that are used to study or screen biological interactions in general. \u003cbr\u003e Arranged in three parts, the text begins by reviewing techniques nowadays almost considered classical, such as affinity chromatography and ultrafiltration, as well as the latest techniques. The second part focusses on all MS-based methods for the study of interactions of proteins with all classes of biomolecules. Besides pull down-based approaches, this section also emphasizes the use of ion mobility MS, capture-compound approaches, chemical proteomics and interactomics. The third and final part discusses other important technologies frequently employed in interaction studies, such as biosensors and microarrays.\u003cbr\u003e For pharmaceutical, analytical, protein, environmental and biochemists, as well as those working in pharmaceutical and analytical laboratories.\u003cbr\u003e\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTrade Review\u003c\/b\u003e\u003cbr\u003e\"Illustrated with beautiful artwork, the book presents a combination of topics that will be useful to inspire new work.\" (Analytical and Bioanalytical Chemistry 2016)\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003eList of Contributors XIII\u003c\/p\u003e \u003cp\u003ePreface XVII\u003c\/p\u003e \u003cp\u003eAbbreviations XIX\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Introduction to Mass Spectrometry, a Tutorial 1\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eWilfried M.A. Niessen and David Falck\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Introduction 1\u003c\/p\u003e \u003cp\u003e1.2 Figures of Merit 1\u003c\/p\u003e \u003cp\u003e1.2.1 Introduction 1\u003c\/p\u003e \u003cp\u003e1.2.2 Resolution 2\u003c\/p\u003e \u003cp\u003e1.2.3 Mass Accuracy 4\u003c\/p\u003e \u003cp\u003e1.2.4 General Data Acquisition in MS 5\u003c\/p\u003e \u003cp\u003e1.3 Analyte Ionization 6\u003c\/p\u003e \u003cp\u003e1.3.1 Introduction 6\u003c\/p\u003e \u003cp\u003e1.3.2 Electrospray Ionization 8\u003c\/p\u003e \u003cp\u003e1.3.3 Matrix-Assisted Laser Desorption Ionization 10\u003c\/p\u003e \u003cp\u003e1.3.4 Other Ionization Methods 10\u003c\/p\u003e \u003cp\u003e1.3.5 Solvent and Sample Compatibility Issues 11\u003c\/p\u003e \u003cp\u003e1.4 Mass Analyzer Building Blocks 12\u003c\/p\u003e \u003cp\u003e1.4.1 Introduction 12\u003c\/p\u003e \u003cp\u003e1.4.2 Quadrupole Mass Analyzer 13\u003c\/p\u003e \u003cp\u003e1.4.3 Ion-Trap Mass Analyzer 13\u003c\/p\u003e \u003cp\u003e1.4.4 Time-of-Flight Mass Analyzer 15\u003c\/p\u003e \u003cp\u003e1.4.5 Fourier Transform Ion Cyclotron Resonance Mass Spectrometer 16\u003c\/p\u003e \u003cp\u003e1.4.6 Orbitrap Mass Analyzer 17\u003c\/p\u003e \u003cp\u003e1.4.7 Ion Detection 18\u003c\/p\u003e \u003cp\u003e1.5 Tandem Mass Spectrometry 18\u003c\/p\u003e \u003cp\u003e1.5.1 Introduction: “Tandem-in-Time” and “Tandem-in-Space” 18\u003c\/p\u003e \u003cp\u003e1.5.2 Ion Dissociation Techniques 20\u003c\/p\u003e \u003cp\u003e1.5.3 Tandem Quadrupole MS–MS Instruments 21\u003c\/p\u003e \u003cp\u003e1.5.4 Ion-Trap MSn Instruments 23\u003c\/p\u003e \u003cp\u003e1.5.5 Tandem TOF (TOF–TOF) Instruments 23\u003c\/p\u003e \u003cp\u003e1.5.6 Hybrid Instruments (Q–TOF, Q–LIT, IT–TOF) 24\u003c\/p\u003e \u003cp\u003e1.5.7 MS–MS and MSn in FT-ICR-MS 26\u003c\/p\u003e \u003cp\u003e1.5.8 Orbitrap-Based Hybrid Systems 27\u003c\/p\u003e \u003cp\u003e1.5.9 Ion-Mobility Spectrometry–Mass Spectrometry 28\u003c\/p\u003e \u003cp\u003e1.6 Data Interpretation and Analytical Strategies 30\u003c\/p\u003e \u003cp\u003e1.6.1 Data Acquisition in MS Revisited 30\u003c\/p\u003e \u003cp\u003e1.6.2 Quantitative Bioanalysis and Residue Analysis 31\u003c\/p\u003e \u003cp\u003e1.6.3 Identification of Small-Molecule “Known Unknowns” 32\u003c\/p\u003e \u003cp\u003e1.6.4 Identification of Drug Metabolites 33\u003c\/p\u003e \u003cp\u003e1.6.5 Protein Molecular Weight Determination 37\u003c\/p\u003e \u003cp\u003e1.6.6 Peptide Fragmentation and Sequencing 38\u003c\/p\u003e \u003cp\u003e1.6.7 General Proteomics Strategies: Top-Down, Middle-Down, Bottom-Up 39\u003c\/p\u003e \u003cp\u003e1.7 Conclusion and Perspectives 43\u003c\/p\u003e \u003cp\u003eReferences 43\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart I Direct MS Based Affinity Techniques 55\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Studying Protein–Protein Interactions by Combining Native Mass Spectrometry and Chemical Cross-Linking 57\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eMichal Sharon and Andrea Sinz\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction 57\u003c\/p\u003e \u003cp\u003e2.2 Protein Analysis by Mass Spectrometry 58\u003c\/p\u003e \u003cp\u003e2.3 Native MS 59\u003c\/p\u003e \u003cp\u003e2.3.1 Instrumentation for High-mass ion Detection 60\u003c\/p\u003e \u003cp\u003e2.3.2 Defining the Exact Mass of the Composing Subunits 60\u003c\/p\u003e \u003cp\u003e2.3.3 Analyzing the Intact Complex 61\u003c\/p\u003e \u003cp\u003e2.4 Chemical Cross-linking MS 64\u003c\/p\u003e \u003cp\u003e2.4.1 Types of Cross-linkers 64\u003c\/p\u003e \u003cp\u003e2.4.2 MS\/MS Cleavable Cross-linkers 66\u003c\/p\u003e \u003cp\u003e2.4.3 Data Analysis 68\u003c\/p\u003e \u003cp\u003e2.5 Value of Combining NativeMS with Chemical Cross-linkingMS 68\u003c\/p\u003e \u003cp\u003e2.6 Regulating the Giant 69\u003c\/p\u003e \u003cp\u003e2.7 Capturing Transient Interactions 70\u003c\/p\u003e \u003cp\u003e2.8 An Integrative Approach for Obtaining Low-Resolution Structures of Native Protein Complexes 72\u003c\/p\u003e \u003cp\u003e2.9 Future Directions 73\u003c\/p\u003e \u003cp\u003eReferences 74\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Native Mass Spectrometry Approaches Using Ion Mobility-Mass Spectrometry 81\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eFrederik Lermyte, Esther Marie Martin, Albert Konijnenberg, Filip Lemière, and Frank Sobott\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 81\u003c\/p\u003e \u003cp\u003e3.2 Sample Preparation 82\u003c\/p\u003e \u003cp\u003e3.3 Electrospray Ionization 84\u003c\/p\u003e \u003cp\u003e3.4 Mass Analyzers and Tandem MS Approaches 88\u003c\/p\u003e \u003cp\u003e3.5 Ion Mobility 90\u003c\/p\u003e \u003cp\u003e3.6 Data Processing 95\u003c\/p\u003e \u003cp\u003e3.7 Challenges and Future Perspectives 98\u003c\/p\u003e \u003cp\u003eReferences 102\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart II LC–MS Based with Indirect Assays 109\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Methodologies for Effect-Directed Analysis: Environmental Applications, Food Analysis, and Drug Discovery 111\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eWillem Jonker, Marja Lamoree, Corine J. Houtman, and Jeroen Kool\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction 111\u003c\/p\u003e \u003cp\u003e4.2 Principle of Traditional Effect-Directed Analysis 113\u003c\/p\u003e \u003cp\u003e4.3 Sample Preparation 113\u003c\/p\u003e \u003cp\u003e4.3.1 Environmental Analysis 113\u003c\/p\u003e \u003cp\u003e4.3.2 Food Analysis 121\u003c\/p\u003e \u003cp\u003e4.3.3 Drug Discovery 124\u003c\/p\u003e \u003cp\u003e4.4 Fractionation for Bioassay Testing 126\u003c\/p\u003e \u003cp\u003e4.4.1 Environmental Analysis 126\u003c\/p\u003e \u003cp\u003e4.4.2 Food Analysis 130\u003c\/p\u003e \u003cp\u003e4.4.3 Drug Discovery 131\u003c\/p\u003e \u003cp\u003e4.5 Miscellaneous Approaches 133\u003c\/p\u003e \u003cp\u003e4.6 Bioassay Testing 136\u003c\/p\u003e \u003cp\u003e4.6.1 Environmental Analysis 136\u003c\/p\u003e \u003cp\u003e4.6.2 Food Analysis 140\u003c\/p\u003e \u003cp\u003e4.6.3 Drug Discovery 140\u003c\/p\u003e \u003cp\u003e4.7 Identification and Confirmation Process 141\u003c\/p\u003e \u003cp\u003e4.7.1 Instrumentation 141\u003c\/p\u003e \u003cp\u003e4.7.2 Data Analysis 143\u003c\/p\u003e \u003cp\u003e4.8 Conclusion and Perspectives 148\u003c\/p\u003e \u003cp\u003eReferences 149\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 MS Binding Assays 165\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eGeorg Höfner and Klaus T.Wanner\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction 165\u003c\/p\u003e \u003cp\u003e5.2 MS Binding Assays – Strategy 167\u003c\/p\u003e \u003cp\u003e5.2.1 Analogies and Differences Compared to Radioligand Binding Assays 167\u003c\/p\u003e \u003cp\u003e5.2.2 Fundamental Assay Considerations 169\u003c\/p\u003e \u003cp\u003e5.2.3 Fundamental Analytical Considerations 170\u003c\/p\u003e \u003cp\u003e5.3 Application of MS Binding Assays 171\u003c\/p\u003e \u003cp\u003e5.3.1 MS Binding Assays for the GABA Transporter GAT1 171\u003c\/p\u003e \u003cp\u003e5.3.2 MS Binding Assays for the Serotonin Transporter 183\u003c\/p\u003e \u003cp\u003e5.3.3 MS Binding Assays Based on the Quantitation of the Nonbound Marker 187\u003c\/p\u003e \u003cp\u003e5.3.4 Other Examples Following the Concept of MS Binding Assays 189\u003c\/p\u003e \u003cp\u003e5.4 Summary and Perspectives 191\u003c\/p\u003e \u003cp\u003eAcknowledgments 192\u003c\/p\u003e \u003cp\u003eReferences 192\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Metabolic Profiling Approaches for the Identification of Bioactive Metabolites in Plants 199\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eEmily Pipan and Angela I. Calderón\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction to Plant Metabolic Profiling 199\u003c\/p\u003e \u003cp\u003e6.2 Sample Collection and Processing 200\u003c\/p\u003e \u003cp\u003e6.3 Hyphenated Techniques 203\u003c\/p\u003e \u003cp\u003e6.3.1 Liquid Chromatography–Mass Spectrometry 203\u003c\/p\u003e \u003cp\u003e6.3.2 Gas Chromatography–Mass Spectrometry 206\u003c\/p\u003e \u003cp\u003e6.3.3 Capillary Electrophoresis–Mass Spectrometry 207\u003c\/p\u003e \u003cp\u003e6.4 Mass Spectrometry 207\u003c\/p\u003e \u003cp\u003e6.4.1 Time of Flight 208\u003c\/p\u003e \u003cp\u003e6.4.2 Quadrupole Mass Filter 208\u003c\/p\u003e \u003cp\u003e6.4.3 Ion Traps (Orbitrap and Linear Quadrupole (LTQ)) 209\u003c\/p\u003e \u003cp\u003e6.4.4 Fourier Transform Mass Spectrometry 210\u003c\/p\u003e \u003cp\u003e6.4.5 Ion Mobility Mass Spectrometry 210\u003c\/p\u003e \u003cp\u003e6.5 Mass Spectrometric Imaging 210\u003c\/p\u003e \u003cp\u003e6.5.1 MALDI-MS 211\u003c\/p\u003e \u003cp\u003e6.5.2 SIMS-MS 212\u003c\/p\u003e \u003cp\u003e6.5.3 DESI-MS 212\u003c\/p\u003e \u003cp\u003e6.5.4 LAESI-MS 213\u003c\/p\u003e \u003cp\u003e6.5.5 LDI-MS and Others for Imaging 213\u003c\/p\u003e \u003cp\u003e6.6 Data Analysis 214\u003c\/p\u003e \u003cp\u003e6.6.1 Data Processing 214\u003c\/p\u003e \u003cp\u003e6.6.2 Data Analysis Methods 214\u003c\/p\u003e \u003cp\u003e6.6.3 Databases 215\u003c\/p\u003e \u003cp\u003e6.7 Future Perspectives 216\u003c\/p\u003e \u003cp\u003eReferences 216\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Antivenomics: A Proteomics Tool for Studying the Immunoreactivity of Antivenoms 227\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJuan J. Calvete, José María Gutiérrez, Libia Sanz, Davinia Pla, and Bruno Lomonte\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction 227\u003c\/p\u003e \u003cp\u003e7.2 Challenge of Fighting Human Envenoming by Snakebites 227\u003c\/p\u003e \u003cp\u003e7.3 Toolbox for Studying the Immunological Profile of Antivenoms 228\u003c\/p\u003e \u003cp\u003e7.4 First-Generation Antivenomics 229\u003c\/p\u003e \u003cp\u003e7.5 Snake Venomics 230\u003c\/p\u003e \u003cp\u003e7.6 Second-Generation Antivenomics 232\u003c\/p\u003e \u003cp\u003e7.7 Concluding Remarks 236\u003c\/p\u003e \u003cp\u003eAcknowledgments 236\u003c\/p\u003e \u003cp\u003eReferences 236\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart III Direct Pre- and On-Column Coupled Techniques 241\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Frontal and Zonal Affinity Chromatography Coupled to Mass Spectrometry 243\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eNagendra S. Singh, Zhenjing Jiang, and Ruin Moaddel\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction 243\u003c\/p\u003e \u003cp\u003e8.2 Frontal Affinity Chromatography 244\u003c\/p\u003e \u003cp\u003e8.3 Staircase Method 247\u003c\/p\u003e \u003cp\u003e8.4 Simultaneous Frontal Analysis of a Complex Mixture 249\u003c\/p\u003e \u003cp\u003e8.5 Multiprotein Stationary Phase 252\u003c\/p\u003e \u003cp\u003e8.6 Zonal Chromatography 253\u003c\/p\u003e \u003cp\u003e8.7 Nonlinear Chromatography 260\u003c\/p\u003e \u003cp\u003eAcknowledgments 265\u003c\/p\u003e \u003cp\u003eReferences 265\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Online Affinity Assessment and Immunoaffinity Sample Pretreatment in Capillary Electrophoresis–Mass Spectrometry 271\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRob Haselberg and Govert W. Somsen\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction 271\u003c\/p\u003e \u003cp\u003e9.2 Capillary Electrophoresis 272\u003c\/p\u003e \u003cp\u003e9.3 Affinity Capillary Electrophoresis 276\u003c\/p\u003e \u003cp\u003e9.3.1 Dynamic Equilibrium ACE (Fast Complexation Kinetics) 276\u003c\/p\u003e \u003cp\u003e9.3.2 Pre-Equilibrium ACE (Slow Complexation Kinetics) 279\u003c\/p\u003e \u003cp\u003e9.3.3 Kinetic ACE (Intermediate Complexation Kinetics) 280\u003c\/p\u003e \u003cp\u003e9.4 Immunoaffinity Capillary Electrophoresis 281\u003c\/p\u003e \u003cp\u003e9.5 Capillary Electrophoresis–Mass Spectrometry 283\u003c\/p\u003e \u003cp\u003e9.5.1 General Requirements for Effective CE–MS Coupling 283\u003c\/p\u003e \u003cp\u003e9.5.2 Specific Requirements for ACE–MS and IA-CE-MS 284\u003c\/p\u003e \u003cp\u003e9.6 Application of ACE–MS 286\u003c\/p\u003e \u003cp\u003e9.7 Applications of IA-CE–MS 292\u003c\/p\u003e \u003cp\u003e9.8 Conclusions 295\u003c\/p\u003e \u003cp\u003eReferences 296\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Label-Free Biosensor Affinity Analysis Coupled to Mass Spectrometry 299\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eDavid Bonnel, Dora Mehn, and Gerardo R. Marchesini\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction to MS-Coupled Biosensor Platforms 299\u003c\/p\u003e \u003cp\u003e10.2 Strategies for Coupling Label-Free Analysis with Mass Spectrometry 301\u003c\/p\u003e \u003cp\u003e10.2.1 On-Chip Approaches 301\u003c\/p\u003e \u003cp\u003e10.2.2 Off-Chip Configurations 305\u003c\/p\u003e \u003cp\u003e10.2.3 Chip Capture and Release Chromatography – Electrospray-MS 306\u003c\/p\u003e \u003cp\u003e10.3 New Sensor and MS Platforms, Opportunities for Integration 307\u003c\/p\u003e \u003cp\u003e10.3.1 Imaging Nanoplasmonics 307\u003c\/p\u003e \u003cp\u003e10.3.2 EvanescentWave SiliconWaveguides 308\u003c\/p\u003e \u003cp\u003e10.3.3 New Trends in MS Matrix-Free Ion Sources 309\u003c\/p\u003e \u003cp\u003e10.3.4 Tag-Mass 310\u003c\/p\u003e \u003cp\u003e10.3.5 Integration 310\u003c\/p\u003e \u003cp\u003eReferences 310\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart IV Direct Post Column Coupled Affinity Techniques 317\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 High-Resolution Screening: Post-Column Continuous-Flow Bioassays 319\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eDavid Falck,Wilfried M.A. Niessen, and Jeroen Kool\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction 319\u003c\/p\u003e \u003cp\u003e11.1.1 Variants of On-line Post-Column Assays Using Mass Spectrometry 321\u003c\/p\u003e \u003cp\u003e11.1.2 Targets and Analytes 328\u003c\/p\u003e \u003cp\u003e11.2 The High-Resolution Screening Platform 330\u003c\/p\u003e \u003cp\u003e11.2.1 Separation 330\u003c\/p\u003e \u003cp\u003e11.2.2 Flow Splitting 334\u003c\/p\u003e \u003cp\u003e11.2.3 Bioassay 336\u003c\/p\u003e \u003cp\u003e11.2.4 MS Detection 340\u003c\/p\u003e \u003cp\u003e11.3 Data Analysis 342\u003c\/p\u003e \u003cp\u003e11.3.1 Differences between HRS and HTS 342\u003c\/p\u003e \u003cp\u003e11.3.2 Validation 350\u003c\/p\u003e \u003cp\u003e11.4 Conclusions and Perspectives 353\u003c\/p\u003e \u003cp\u003e11.4.1 The Relation of On-line Post-Column Assays to Other Formats 353\u003c\/p\u003e \u003cp\u003e11.4.2 Trends in High-Resolution Screening 354\u003c\/p\u003e \u003cp\u003e11.4.3 Conclusions 357\u003c\/p\u003e \u003cp\u003eReferences 358\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Conclusions 365\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJeroen Kool\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIndex 373\u003c\/p\u003e","brand":"Wiley-VCH Verlag GmbH","offers":[{"title":"Default Title","offer_id":51742969069911,"sku":"9783527334643","price":999.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9783527334643.jpg?v=1758387708","url":"https:\/\/bookcurl.com\/products\/analyzing-biomolecular-interactions-by-mass-spectrometry-9783527334643","provider":"Book Curl","version":"1.0","type":"link"}