Analysis of Protein Post-Translational Modifications by Mass Spectrometry

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John Wiley & Sons, Oct 12, 2016 - Science - 416 pages
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  • 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
 

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Contents

Chapter 1 Introduction
1
Chapter 2 Identification and Analysis of Protein Phosphorylation by Mass Spectrometry
17
Chapter 3 Analysis of Protein Glycosylation by Mass Spectrometry
89
Chapter 4 Protein Acetylation and Methylation
161
Chapter 5 Tyrosine Nitration
197
Chapter 6 Mass Spectrometry Methods for the Analysis of Isopeptides Generated from Mammalian Protein Ubiquitination and SUMOylation
235
Chapter 7 The Deimination of Arginine to Citrulline
275
Chapter 8 Glycation of Proteins
307
Chapter 9 Biological Significance and Analysis of Tyrosine Sulfation
333
Chapter 10 The Application of Mass Spectrometry for the Characterization of Monoclonal AntibodyBased Therapeutics
351
Index
387
EULA
396
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About the author (2016)

John Griffiths is an analytical chemist with 30 years experience in the analysis of a wide range of analytes using mass spectrometry and other techniques. For the past 13 years, John has focused solely on the application of mass spectrometry to the analysis of peptides and proteins – proteomics. John has published multiple papers on biological mass spectrometry and has presented his work at both national and international conferences. John has a particular interest in the analysis of PTMs and has developed a number of strategies, such as the MIDAS with Richard Unwin, to enhance their detection. John is also the director of a mass spectrometry training and consultancy enterprise, MS-Insight Ltd.

Richard Unwin is a biochemist and mass spectrometrist with over 18 years’ experience in the field of proteomics, in particular the quantification and characterization of proteins by mass spectrometry. Richard was among the first to develop the use of iTRAQ technology for protein quantitation and, with John Griffiths, was also amongst the first researchers to begin to realize the potential of multiple reaction monitoring MS for the discovery and characterization of post-translational modifications. Richard has contributed chapters on proteomics methods for a number of textbooks, aimed at both practicing mass spectrometrists and undergraduates, and has authored over 40 papers in the field.

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