Proteomics of Biological Systems Protein Phosphorylation Using Mass Spectrometry Techniques

About this book

Phosphorylation is the addition of a phosphate (PO4) group to a protein or other organic molecule. Phosphorylation activates or deactivates many protein enzymes, causing or preventing the mechanisms of diseases such as cancer and diabetes. This book shows how to use mass spectrometry to determine whether or not a protein has been correctly modified by the addition of a phospate group. The book provides a combination of detailed step-by-step methodology for phosphoproteomic sample preparation, mass spectral instrumental analysis, and data interpretation approaches. It also includes the use of bioinformatic internet tools such as the Blast2GO gene ontology (GO) tool, used to help understand and interpret complex data collected during these studies.

Contents

Preface
Acknowledgements
Dedication
Glossary, Abbreviations, and Definitions

1. Post Translational Modification of Proteins (PTM)
2. Glycosylation of Proteins
3. Sulfation of Proteins as Post Translational Modification
4. Eukaryote PTM as Phosohorylation: Normal State Studies
5. Eukaryote PTM as Phosphorylation: Perturbed State Studies
6. Prokaryotic Phosphorylation of Serine, Threonine, and Tyrosine
7. Prokaryotic Phosphorylation of Histidine

Appendix I. Atomic Weights and Isotopic Compositions
Appendix II. Periodic Table
Appendix III. Fundamental Physical Constants
Index

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Biography

BRYAN M. HAM, PhD, is a member of the American Society for Mass Spectrometry and the American Chemical Society. He has conducted proteomics and lipidomics research at The Ohio State University and Pacific Northwest National Laboratory in Richland, Washington. He is currently working for the Department of Homeland Security at the U.S. Customs and Border Protection New York Laboratory. He has published numerous research papers in peer-reviewed journals, and is the author of Even Electron Mass Spectrometry with Biomolecule Applications (Wiley).