Analysis of Protein Post-Translational Modifications by Mass Spectrometry [Hardcover]

• 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

List of Contributors xi

Preface xv

1 Introduction 1
Rebecca Pferdehirt, Florian Gnad and Jennie R. Lill

1.1 Post-translational Modification of Proteins 1

1.2 Global versus Targeted Analysis Strategies 3

1.3 Mass Spectrometric Analysis Methods for the Detection of PTMs 5

1.3.1 Data?-Dependent and Data?-Independent Analyses 6

1.3.2 Targeted Analyses 7

1.3.3 Multiple Reaction Monitoring 8

1.3.4 Multiple Reaction Monitoring Initiated Detection and Sequencing 9

1.4 The Importance of Bioinformatics 9

Acknowledgements 11

References 11

2 Identification and Analysis of Protein Phosphorylation by Mass Spectrometry 17
Dean E. McNulty, Timothy W. Sikorski and Roland S. Annan

2.1 Introduction to Protein Phosphorylation 17

2.2 Analysis of Protein Phosphorylation by Mass Spectrometry 25

2.3 Global Analysis of Protein Phosphorylation by Mass Spectrometry 39

2.4 Sample Preparation and Enrichment Strategies for Phosphoprotein Analysis by Mass Spectrometry 46

2.5 Multidimensional Separations for Deep Coverage of the Phosphol2