{"product_id":"analysis-of-protein-posttranslational-modifications-by-mass-spectrometry-9781119045854","title":"Analysis of Protein PostTranslational","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e\u003cul\u003e \u003cli\u003eCovers all major modifications, including phosphorylation, glycosylation, acetylation, ubiquitination, sulfonation and and glycation\u003c\/li\u003e \u003cli\u003eDiscussion of the chemistry behind each modification, along with key methods and references\u003c\/li\u003e \u003cli\u003eContributions from some of the leading researchers in the field\u003c\/li\u003e \u003cli\u003eA valuable reference source for all laboratories undertaking proteomics, mass spectrometry and post-translational modification research\u003c\/li\u003e \u003c\/ul\u003e\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003eList of Contributors xi\u003c\/p\u003e \u003cp\u003ePreface xv\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Introduction 1\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRebecca Pferdehirt, Florian Gnad and Jennie R. Lill\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Post-translational Modification of Proteins 1\u003c\/p\u003e \u003cp\u003e1.2 Global versus Targeted Analysis Strategies 3\u003c\/p\u003e \u003cp\u003e1.3 Mass Spectrometric Analysis Methods for the Detection of PTMs 5\u003c\/p\u003e \u003cp\u003e1.3.1 Data-Dependent and Data-Independent Analyses 6\u003c\/p\u003e \u003cp\u003e1.3.2 Targeted Analyses 7\u003c\/p\u003e \u003cp\u003e1.3.3 Multiple Reaction Monitoring 8\u003c\/p\u003e \u003cp\u003e1.3.4 Multiple Reaction Monitoring Initiated Detection and Sequencing 9\u003c\/p\u003e \u003cp\u003e1.4 The Importance of Bioinformatics 9\u003c\/p\u003e \u003cp\u003eAcknowledgements 11\u003c\/p\u003e \u003cp\u003eReferences 11\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Identification and Analysis of Protein Phosphorylation by Mass Spectrometry 17\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eDean E. McNulty, Timothy W. Sikorski and Roland S. Annan\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction to Protein Phosphorylation 17\u003c\/p\u003e \u003cp\u003e2.2 Analysis of Protein Phosphorylation by Mass Spectrometry 25\u003c\/p\u003e \u003cp\u003e2.3 Global Analysis of Protein Phosphorylation by Mass Spectrometry 39\u003c\/p\u003e \u003cp\u003e2.4 Sample Preparation and Enrichment Strategies for Phosphoprotein Analysis by Mass Spectrometry 46\u003c\/p\u003e \u003cp\u003e2.5 Multidimensional Separations for Deep Coverage of the Phosphoproteome 54\u003c\/p\u003e \u003cp\u003e2.6 Computational and Bioinformatics Tools for Phosphoproteomics 57\u003c\/p\u003e \u003cp\u003e2.7 Concluding Remarks 65\u003c\/p\u003e \u003cp\u003eReferences 66\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Analysis of Protein Glycosylation by Mass Spectrometry 89\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eDavid J. Harvey\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 89\u003c\/p\u003e \u003cp\u003e3.2 General Structures of Carbohydrates 89\u003c\/p\u003e \u003cp\u003e3.2.1 Protein-Linked Glycans 90\u003c\/p\u003e \u003cp\u003e3.3 Isolation and Purification of Glycoproteins 94\u003c\/p\u003e \u003cp\u003e3.3.1 Lectin Affinity Chromatography 95\u003c\/p\u003e \u003cp\u003e3.3.2 Boronate-Based Compounds 95\u003c\/p\u003e \u003cp\u003e3.3.3 Hydrazide Enrichment 96\u003c\/p\u003e \u003cp\u003e3.3.4 Titanium Dioxide Enrichment of Sialylated Glycoproteins 96\u003c\/p\u003e \u003cp\u003e3.4 Mass Spectrometry of Intact Glycoproteins 96\u003c\/p\u003e \u003cp\u003e3.5 Site Analysis 96\u003c\/p\u003e \u003cp\u003e3.6 Glycan Release 98\u003c\/p\u003e \u003cp\u003e3.6.1 Use of Hydrazine 99\u003c\/p\u003e \u003cp\u003e3.6.2 Use of Reductive β-Elimination 99\u003c\/p\u003e \u003cp\u003e3.6.3 Use of Enzymes 100\u003c\/p\u003e \u003cp\u003e3.7 Analysis of Released Glycans 102\u003c\/p\u003e \u003cp\u003e3.7.1 Cleanup of Glycan Samples 102\u003c\/p\u003e \u003cp\u003e3.7.2 Derivatization 102\u003c\/p\u003e \u003cp\u003e3.7.2.1 Derivatization at the Reducing Terminus 102\u003c\/p\u003e \u003cp\u003e3.7.2.2 Derivatization of Hydroxyl Groups: Permethylation 104\u003c\/p\u003e \u003cp\u003e3.7.2.3 Derivatization of Sialic Acids 106\u003c\/p\u003e \u003cp\u003e3.7.3 Exoglycosidase Digestions 106\u003c\/p\u003e \u003cp\u003e3.7.4 HPLC and ESI 107\u003c\/p\u003e \u003cp\u003e3.8 Mass Spectrometry of Glycans 107\u003c\/p\u003e \u003cp\u003e3.8.1 Aspects of Ionization for Mass Spectrometry Specific to the Analysis of Glycans 107\u003c\/p\u003e \u003cp\u003e3.8.1.1 Electron Impact (EI) 107\u003c\/p\u003e \u003cp\u003e3.8.1.2 Fast Atom Bombardment (FAB) 108\u003c\/p\u003e \u003cp\u003e3.8.1.3 Matrix-Assisted Laser Desorption\/Ionization (MALDI) 108\u003c\/p\u003e \u003cp\u003e3.8.1.4 Electrospray Ionization (ESI) 113\u003c\/p\u003e \u003cp\u003e3.8.2 Glycan Composition by Mass Spectrometry 114\u003c\/p\u003e \u003cp\u003e3.8.3 Fragmentation 114\u003c\/p\u003e \u003cp\u003e3.8.3.1 Nomenclature of Fragment Ions 116\u003c\/p\u003e \u003cp\u003e3.8.3.2 In-Source Decay (ISD) Ions 116\u003c\/p\u003e \u003cp\u003e3.8.3.3 Postsource Decay (PSD) Ions 117\u003c\/p\u003e \u003cp\u003e3.8.3.4 Collision-Induced Dissociation (CID) 117\u003c\/p\u003e \u003cp\u003e3.8.3.5 Electron Transfer Dissociation (ETD) 118\u003c\/p\u003e \u003cp\u003e3.8.3.6 Infrared Multiphoton Dissociation (IRMPD) 118\u003c\/p\u003e \u003cp\u003e3.8.3.7 MSn 118\u003c\/p\u003e \u003cp\u003e3.8.3.8 Fragmentation Modes of Different Ion Types 119\u003c\/p\u003e \u003cp\u003e3.8.4 Ion Mobility 126\u003c\/p\u003e \u003cp\u003e3.8.5 Quantitative Measurements 128\u003c\/p\u003e \u003cp\u003e3.9 Computer Interpretation of MS Data 128\u003c\/p\u003e \u003cp\u003e3.10 Total Glycomics Methods 130\u003c\/p\u003e \u003cp\u003e3.11 Conclusions 131\u003c\/p\u003e \u003cp\u003eAbbreviations 131\u003c\/p\u003e \u003cp\u003eReferences 133\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Protein Acetylation and Methylation 161\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eCaroline Evans\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Overview of Protein Acetylation and Methylation 161\u003c\/p\u003e \u003cp\u003e4.1.1 Protein Acetylation 161\u003c\/p\u003e \u003cp\u003e4.1.2 Protein Methylation 162\u003c\/p\u003e \u003cp\u003e4.1.3 Functional Aspects 163\u003c\/p\u003e \u003cp\u003e4.1.4 Mass Spectrometry Analysis 163\u003c\/p\u003e \u003cp\u003e4.2 Mass Spectrometry Behavior of Modified Peptides 164\u003c\/p\u003e \u003cp\u003e4.2.1 MS Fragmentation Modes 164\u003c\/p\u003e \u003cp\u003e4.2.2 Acetylation- and Methylation-Specific Diagnostic Ions in MS Analysis 165\u003c\/p\u003e \u003cp\u003e4.2.3 Application of MS Methodologies for the Analysis of PTM Status 168\u003c\/p\u003e \u003cp\u003e4.2.4 Quantification Strategies 169\u003c\/p\u003e \u003cp\u003e4.2.4.1 Single Reaction Monitoring\/Multiple Reaction Monitoring 170\u003c\/p\u003e \u003cp\u003e4.2.4.2 Parallel Reaction Monitoring 171\u003c\/p\u003e \u003cp\u003e4.2.4.3 Data-Independent Acquisition MS 172\u003c\/p\u003e \u003cp\u003e4.2.4.4 Ion Mobility MS 173\u003c\/p\u003e \u003cp\u003e4.2.5 Use of Stable Isotope–Labeled Precursors 174\u003c\/p\u003e \u003cp\u003e4.2.5.1 Dynamics of Acetylation and Methylation 174\u003c\/p\u003e \u003cp\u003e4.2.5.2 Stoichiometry of Acetylation and Methylation 175\u003c\/p\u003e \u003cp\u003e4.3 Global Analysis 176\u003c\/p\u003e \u003cp\u003e4.3.1 Top-Down Proteomics 176\u003c\/p\u003e \u003cp\u003e4.3.2 Middle Down 177\u003c\/p\u003e \u003cp\u003e4.4 Enrichment 178\u003c\/p\u003e \u003cp\u003e4.4.1 Immunoaffinity Enrichment 178\u003c\/p\u003e \u003cp\u003e4.4.2 Reader Domain-Based Capture 179\u003c\/p\u003e \u003cp\u003e4.4.2.1 Kac-Specific Capture Reagents 179\u003c\/p\u003e \u003cp\u003e4.4.2.2 Methyl-Specific Capture Reagents 180\u003c\/p\u003e \u003cp\u003e4.4.3 Biotin Switch-Based Capture 180\u003c\/p\u003e \u003cp\u003e4.4.4 Enrichment of N-Terminally Acetylated Peptides 181\u003c\/p\u003e \u003cp\u003e4.5 Bioinformatics 181\u003c\/p\u003e \u003cp\u003e4.5.1 Assigning Acetylation and Methylation Status 182\u003c\/p\u003e \u003cp\u003e4.5.2 PTM Repositories and Data Mining Tools 183\u003c\/p\u003e \u003cp\u003e4.5.3 Computational Prediction Tools for Acetylation and Methylation Sites 183\u003c\/p\u003e \u003cp\u003e4.5.4 Information for Design of Follow-Up Experiments 185\u003c\/p\u003e \u003cp\u003e4.6 Summary 185\u003c\/p\u003e \u003cp\u003eReferences 185\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Tyrosine Nitration 197\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eXianquan Zhan, Ying Long and Dominic M. Desiderio\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Overview of Tyrosine Nitration 197\u003c\/p\u003e \u003cp\u003e5.2 MS Behavior of Nitrated Peptides 199\u003c\/p\u003e \u003cp\u003e5.3 Global Analysis of Tyrosine Nitration 208\u003c\/p\u003e \u003cp\u003e5.4 Enrichment Strategies 214\u003c\/p\u003e \u003cp\u003e5.5 Concluding Remarks 221\u003c\/p\u003e \u003cp\u003eAcknowledgements 222\u003c\/p\u003e \u003cp\u003eAbbreviations 222\u003c\/p\u003e \u003cp\u003eReferences 223\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Mass Spectrometry Methods for the Analysis of Isopeptides Generated from Mammalian Protein Ubiquitination and SUMOylation 235\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eNavin Chicooree and Duncan L. Smith\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Overview of Ub and SUMO 235\u003c\/p\u003e \u003cp\u003e6.1.1 Biological Overview of Ubiquitin-Like Proteins 235\u003c\/p\u003e \u003cp\u003e6.1.2 Biological Overview of Ub and SUMO 236\u003c\/p\u003e \u003cp\u003e6.1.3 Biological Functions of Ub and SUMO 236\u003c\/p\u003e \u003cp\u003e6.2 Mass Spectrometry Behavior of Isopeptides 237\u003c\/p\u003e \u003cp\u003e6.2.1 Terminology of a Ub\/Ubl isopeptide 237\u003c\/p\u003e \u003cp\u003e6.2.2 Mass Spectrometry Analysis of SUMO-Isopeptides Derived from Proteolytic Digestion 238\u003c\/p\u003e \u003cp\u003e6.2.3 Analysis of SUMO-Isopeptides with Typical Full-Length Tryptic Iso-chains 238\u003c\/p\u003e \u003cp\u003e6.2.4 Analysis of SUMO-Isopeptides with Atypical Tryptic Iso-chains and Shorter Iso-chains Derived from Alternative Digestion Strategies 244\u003c\/p\u003e \u003cp\u003e6.2.4.1 SUMO-Isopeptides with Atypical Iso-chains Generated from Tryptic Digestion 244\u003c\/p\u003e \u003cp\u003e6.2.4.2 Dual Proteolytic Enzyme Digestion with Trypsin and Chymotrypsin 247\u003c\/p\u003e \u003cp\u003e6.2.4.3 Proteolytic Enzyme and Chemical Digestion with Trypsin and Acid 248\u003c\/p\u003e \u003cp\u003e6.2.5 MS Analysis of Modified Ub- and SUMO-Isopeptides under CID Conditions 250\u003c\/p\u003e \u003cp\u003e6.2.6 SPITC Modification 251\u003c\/p\u003e \u003cp\u003e6.2.7 Dimethyl Modification 252\u003c\/p\u003e \u003cp\u003e6.2.8 m-TRAQ Modification 256\u003c\/p\u003e \u003cp\u003e6.3 Enrichment and Global Analysis of Isopeptides 259\u003c\/p\u003e \u003cp\u003e6.3.1 Overview of Enrichment Approaches 259\u003c\/p\u003e \u003cp\u003e6.3.2 K-GG Antibody 260\u003c\/p\u003e \u003cp\u003e6.3.3 COFRADIC 262\u003c\/p\u003e \u003cp\u003e6.3.4 SUMOylation Enrichment 263\u003c\/p\u003e \u003cp\u003e6.4 Concluding Remarks and Recommendations 265\u003c\/p\u003e \u003cp\u003eReferences 267\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 The Deimination of Arginine to Citrulline 275\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eAndrew J. Creese and Helen J. Cooper\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Overview of Arginine to Citrulline Conversion: Biological Importance 275\u003c\/p\u003e \u003cp\u003e7.2 Mass Spectrometry-Based Proteomics 279\u003c\/p\u003e \u003cp\u003e7.3 Liquid Chromatography and Mass Spectrometry Behavior of Citrullinated Peptides 283\u003c\/p\u003e \u003cp\u003e7.4 Global Analysis of Citrullination 288\u003c\/p\u003e \u003cp\u003e7.5 Enrichment Strategies 291\u003c\/p\u003e \u003cp\u003e7.6 Bioinformatics 296\u003c\/p\u003e \u003cp\u003e7.7 Concluding Remarks 297\u003c\/p\u003e \u003cp\u003eAcknowledgements 297\u003c\/p\u003e \u003cp\u003eReferences 297\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Glycation of Proteins 307\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eNaila Rabbani and Paul J. Thornalley\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Overview of Protein Glycation 307\u003c\/p\u003e \u003cp\u003e8.2 Mass Spectrometry Behavior of Glycated Peptides 315\u003c\/p\u003e \u003cp\u003e8.3 Global Analysis of Glycation 318\u003c\/p\u003e \u003cp\u003e8.4 Enrichment Strategies 319\u003c\/p\u003e \u003cp\u003e8.5 Bioinformatics 320\u003c\/p\u003e \u003cp\u003e8.6 Concluding Remarks 323\u003c\/p\u003e \u003cp\u003eAcknowledgements 324\u003c\/p\u003e \u003cp\u003eReferences 324\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Biological Significance and Analysis of Tyrosine Sulfation 333\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eÉva Klement, Éva Hunyadi-Gulyás and Katalin F. Medzihradszky\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Overview of Protein Sulfation 333\u003c\/p\u003e \u003cp\u003e9.2 Mass Spectrometry Behavior of Sulfated Peptides 334\u003c\/p\u003e \u003cp\u003e9.3 Enrichment Strategies and Global Analysis of Sulfation 340\u003c\/p\u003e \u003cp\u003e9.4 Sulfation Site Predictions 342\u003c\/p\u003e \u003cp\u003e9.5 Summary 343\u003c\/p\u003e \u003cp\u003eAcknowledgements 344\u003c\/p\u003e \u003cp\u003eReferences 344\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 The Application of Mass Spectrometry for the Characterization of Monoclonal Antibody-Based Therapeutics 351\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRosie Upton, Kamila J. Pacholarz, David Firth, Sian Estdale and Perdita E. Barran\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction 351\u003c\/p\u003e \u003cp\u003e10.1.1 Antibody Structure 352\u003c\/p\u003e \u003cp\u003e10.1.2 N-Linked Glycosylation 354\u003c\/p\u003e \u003cp\u003e10.1.3 Antibody-Drug Conjugates 355\u003c\/p\u003e \u003cp\u003e10.1.4 Biosimilars 356\u003c\/p\u003e \u003cp\u003e10.2 Mass Spectrometry Solutions to Characterizing Monoclonal Antibodies 358\u003c\/p\u003e \u003cp\u003e10.2.1 Hyphenated Mass Spectrometry (X-MS) Techniques to Study Glycosylation Profiles 359\u003c\/p\u003e \u003cp\u003e10.2.2 Hydrogen\/Deuterium Exchange Mass Spectrometry (HDX-MS) to Characterize Monoclonal Antibody Structure 361\u003c\/p\u003e \u003cp\u003e10.2.3 Native Mass Spectrometry and the Use of IM-MS to Probe Monoclonal Antibody Structure 365\u003c\/p\u003e \u003cp\u003e10.3 Advanced Applications 369\u003c\/p\u003e \u003cp\u003e10.3.1 Quantifying Glycosylation 369\u003c\/p\u003e \u003cp\u003e10.3.2 Antibody-Drug Conjugates 370\u003c\/p\u003e \u003cp\u003e10.3.3 Biosimilar Characterization 372\u003c\/p\u003e \u003cp\u003e10.4 Concluding Remarks 374\u003c\/p\u003e \u003cp\u003eReferences 374\u003c\/p\u003e \u003cp\u003eIndex 387\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49528844747095,"sku":"9781119045854","price":107.3,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781119045854.jpg?v=1731873246","url":"https:\/\/bookcurl.com\/products\/analysis-of-protein-posttranslational-modifications-by-mass-spectrometry-9781119045854","provider":"Book Curl","version":"1.0","type":"link"}