Analysis of Protein Post-Translational Modifications by Mass Spectrometry

Analysis of Protein Post-Translational Modifications by Mass Spectrometry by John R. Griffiths, Richard D. Unwin
2016 | ISBN-10: 1119045851 | 416 pages | pdf

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.

great