Analysis of Protein Post-Translational Modifications by Mass Spectrometry

Covers all major modifications, including phosphorylation, glycosylation, acetylation, ubiquitination, sulfonation and and glycation Discussion of the chemistry behind each modification, along with key methods and references Contributions from some of the leading researchers in the field A valuable reference source for all laboratories undertaking proteomics, mass spectrometry and post–translational modification research INDICE: List of contributors .Preface .Chapter 1: Introduction Rebecca Pferdehirt, Florian Gnad, Jennie R. Lill .1.1. Post–translational modification of proteins .1.2. Global versus targeted analysis strategies .1.3. Mass spectrometric analysis methods for the detection of post translational modifications .1.4. The importance of bioinformatics .References .Chapter 2: Identification and Analysis of Protein Phosphorylation by Mass Spectrometry Dean E. McNulty, Timothy W. Sikorski, Roland S. Annan .2.1. Introduction to Protein Phosphorylation .2.2. Analysis of Protein Phosphorylation by Mass Spectrometry .2.3. Global analysis of protein phosphorylation by mass spectrometry .2.4. Sample preparation and enrichment strategies for phosphoprotein analysis by mass spectrometry .2.5. Multidimensional separations for deep coverage of the phosphoproteome .2.6. Computational and bioinformatic tools for phosphoproteomics .2.7. Concluding Remarks .References .Chapter 3: Analysis of Protein Glycosylation by Mass Spectrometry David J. Harvey .3.1. Introduction .3.2. General structures of carbohydrates .3.3. Isolation and purification of glycoproteins .3.4. Mass spectrometry of intact glycoproteins .3.5. Site analysis .3.6. Glycan release .3.7. Analysis of released glycans .3.8. Mass spectrometry of glycans .3.9. Computer interpretation of MS data .3.10. Total glycomics methods .3.11. Conclusions . References .Chapter 4: Protein Acetylation and Methylation Caroline Evans .4.1. Overview of protein acetylation and methylation .4.2. Mass spectrometry behavior of modified peptides .4.3. Global analysis .4.4. Enrichment .4.5. Bioinformatics .4.6. Summary .References .Chapter 5: Tyrosine Nitration Xianquan Zhan, Ying Long, Dominic M. Desiderio .5.1. Overview of tyrosine nitration .5.2. Mass spectrometry behavior of nitrated peptides .5.3. Global analysis of tyrosine nitration .5.4. Enrichment strategies .5.5. Concluding remarks .Abbreviations .Acknowledgements .References .Chapter 6: Mass Spectrometry Methods for the Analysis of Isopeptides Generated from Mammalian Protein Ubiquitination and Sumoylation Navin Chicooree and Duncan L. Smith .6.1. Overview of SUMO and Ub .6.2. Mass Spectrometry Behaviour of Isopeptides .6.3. Enrichment and Global Analysis of Isopeptides .6.4. Concluding Remarks and Recommendations .References .Chapter 7: The Deimination of Arginine to Citrulline Andrew J. Creese, Helen J. Cooper .7.1. Overview of arginine to citrulline conversion: Biological importance .7.2. Mass spectrometry–based proteomics .7.3. Liquid chromatography and mass spectrometry behavior of citrullinated peptides .7.4. Global analysis of citrullination .7.5. Enrichment strategies .7.6. Bioinformatics .7.7. Concluding remarks .Acknowledgements .References .Chapter 8: Glycation of Proteins Naila Rabbani and Paul J. Thornalley .8.1. Overview of protein glycation .8.2. Mass spectrometry behavior of glycated peptides .8.3. Global analysis of glycation .8.4. Enrichment strategies .8.5. Bioinformatics .8.6. Concluding remarks .References .Chapter 9: Biological Significance and Analysis of Tyrosine Sulfation Éva Klement 1, Éva Hundyadi–Gulyás 1, Katalin F. Medzihradszky .9.1. Overview of protein sulfation .9.2. Mass spectrometry behavior of sulfated peptides .9.3. Enrichment strategies and global analysis of sulfation .9.4. Sulfation site predictions .References .Chapter 10: The Application of Mass Spectrometry for the Characterisation of Monoclonal Antibody–Based Therapeutics Rosie Upton, Kamila J. Pacholarz, David Firth, Sian Estdale and Perdita E. Barran .10.1. Introduction .10.2. Antibody Structure .10.3. N–linked Glycosylation .10.4. Antibody–Drug Conjugates .10.5. Biosimilars .10.6. Sorption thermodynamics of heavy metals by ENMs .10.7. Factors influencing heavy metal sorption by ENMs .10.8. Summary and future perspectives .References .Index

• ISBN: 978-1-119-04585-4
• Editorial: Wiley–Blackwell
• Encuadernacion: Cartoné
• Páginas: 416
• Fecha Publicación: 10/11/2016
• Nº Volúmenes: 1
• Idioma: Inglés