This comprehensive volume focuses on the ways in which synthetic peptides have been exploited in order to expand our understanding of the molecular mechanisms involved in protein phosphorylation. It recognizes that virtually all physiological processes are regulated by protein phosphorylation. It discusses the use of synthetic peptides in studying the catalytic mechanism and regulation of protein kinases. It also includes the chemical synthesis of phosphorylated peptides and preparation of specific antisera. This incredible work has lead to the development of a new generation of peptide inhibitors with potencies of greater magnitude than those previously known. Everyone involved with biochemistry and molecular biology will find this one-of-a-kind resource fascinating and filled with useful information.
Table of Contents
1. cAMP-Dependent Protein Kinase: Mechanism for ATP: Protein Phosphotransfer 2. The Inhibitor Protein of the cAMP-Dependent Protein Kinase 3. The SRC Family of Protein-Tyrosine Kinases 4. Myosin Light Chain Kinases 5. Use of Synthetic Peptides to Study Substrate Specificity of Protein Phosphatases 6. Type-2 Casein Kinases: General Properties and Substrate Specificity 7. Substrate Specificity of Cyclic AMP-Dependent Protein Kinase 8. Unique Specificity Determinants for an S6/H4 Kinase and Protein Kinase C: Phosphorylation of Synthetic Peptides Derived from the Smooth Muscle Myosin Light Chain 9. Substrate Specificity of the Cyclic GMP-Dependent Protein Kinase 10. Protein-Tyrosine Kinases 11. Antibodies Against Synthetic Phosphorylation Site Peptides 12. Modern Methods of O-Phosphoserine- and O-Phosphotyrosine-Containing Peptide Synthesis.