Analysis of Protein Post-Translational Modifications by Mass Spectrometry (Wiley Series on Mass Spectrometry) - Tapa dura

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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.

De la contraportada

Provides a comprehensive overview of the various ways mass spectrometry can be used for the detection and analysis of protein post-translational modifications

Post-translational modification of a protein adds significant diversity and function to the proteome. It may involve the addition of functional groups to amino acids, covalent linkage of other proteins or fatty acids, a change in the chemical nature of an amino acid or structural changes resulting from proteolytic cleavage or disulfide bridge formation. Over the last 10 years, mass spectrometry has become a critical tool in the analysis of proteins structure, quantity and modification. Of the 300 or so PTMs known, this book sets out to describe mass spectrometry-based methods for the analysis of some of the most well studied.

Providing a single starting reference point for this growing and important field, with contributions from renowned experts in the analysis of all of the major PTMs and containing key background, references and summarizing the current state-of-the-art, this book is an indispensable tool for students and practitioners of protein mass spectrometry.