Co-and-post-translational Modification of Proteins
Published on 10. February 1994
Book
Hardback
367 pages
978-0-19-505549-8 (ISBN)
Description
This work presents the general biological principles--and the chemical and physical concepts-- needed for an understanding of the post- and co-translational modification of proteins, a fundamental topic in the science of protein biochemistry and molecular biology. Examples of the different types of modification reactions (glycosylation, phosphorylation, prenylation, etc.) are presented to illustrate specific points, and the book is intended to serve as a principles-based guide for studying the subject, whether in the classroom or research laboratory. In addition to its value as a timely overview of a broad, vitally important area, the book can be used in advanced courses on signal transduction, enzymology, and protein chemistry, or as a supplementary text for biochemistry or molecular biology.
More details
Language
English
Place of publication
New York
United States
Target group
College/higher education
Professional and scholarly
Illustrations
halftones, numerous line figures, tables, bibliography
ISBN-13
978-0-19-505549-8 (9780195055498)
Copyright in bibliographic data is held by Nielsen Book Services Limited or its licensors: all rights reserved.
Schweitzer Classification
Persons
Content
PART I: Introduction: General Features of Protein Modification. 1: Reversible and Irreversible Reactions. 2: Co- and Post-Translational Modification. 3: Enzymatic and Non-Enzymatic Reactions. 4: Recombinant Proteins and Enzyme Modification. PART II: Enzymology of Modification. 5: Kinetics of Post-Translational Modification Reactions. 6: Structural Probes of Modifying Enzymes. 7: Reaction Mechanisms. 8: Regulatory Features of Modifying Enzymes. 9: Regulatory Proteins. 10: Autoregulation. 11: Sequential Modifications. 12: Reversibility. PART III: The Protein Substrate. 13: Factors Influencing the Chemical Reactivity of Amino Acid Residues. 14: Structural and Chemical Features of the Substrate. 15: Influence of Neighboring Groups on Modification. 16: Chemical Influences of Side Chains on Modification. 17: Chemical Changes in the Protein Influence Subsequent Post-Translational Modification Reactions. 18: Sequences Distinct from the Modifiable Site Can Influence Modification. 19: Cross- Linking Reactions. 20: The Protein Can Cause its Own Modification. 21: Subunit Structure and Covalent Modification. 22: Sequential Processes and Synergistic Effects. PART IV: The Modified Protein: Isolation and Analysis of Structure. 23: Isolation of Modified Proteins. 24: Amino Acid Analysis of Modified Proteins. 25: Identification of Modified Amino Acids by Physical Methods. 26: Chemical Structure of the Modified Group. 27: Primary Structure of the Modified Site. PART V: Physical and Chemical Properties of Modified Amino Acids. 28: Modification Can Change the Charge of the Protein. 29: Modification Can Change the Hydrophobicity of the Protein. 30: Modification Can Influence Protein Conformation, Folding, and Stability. 31: Flexibility and Function. 32: Modification Can Change Ligand Binding. PART VI: Inhibitors and Activators of Cellular Modification Reactions. 33: Enzyme Inhibitors. 34: Enzyme Activators. PART VII: Biological Effects of Covalent Modification. 35: Reversible and Irreversible Modification. 36: General Criteria for the Biological Role of Protein Modifications. 37: Phosphorylation. 38: Protein Ubiquitination. 39: Covalent Attachment of Long Chain Fatty Acids. 40: Glycosylation. 41: Approaches for the Study of Biological Role. PART I: Introduction: General Features of Protein Modification. 1: Reversible and Irreversible Reactions. 2: Co- and Post-Translational Modification. 3: Enzymatic and Non-Enzymatic Reactions. 4: Recombinant Proteins and Enzyme Modification. PART II: Enzymology of Modification. 5: Kinetics of Post-Translational Modification Reactions. 6: Structural Probes of Modifying Enzymes. 7: Reaction Mechanisms. 8: Regulatory Features of Modifying Enzymes. 9: Regulatory Proteins. 10: Autoregulation. 11: Sequential Modifications. 12: Reversibility. PART III: The Protein Substrate. 13: Factors Influencing the Chemical Reactivity of Amino Acid Residues. 14: Structural and Chemical Features of the Substrate. 15: Influence of Neighboring Groups on Modification. 16: Chemical Influences of Side Chains on Modification. 17: Chemical Changes in the Protein Influence Subsequent Post-Translational Modification Reactions. 18: Sequences Distinct from the Modifiable Site Can Influence Modification. 19: Cross- Linking Reactions. 20: The Protein Can Cause its Own Modification. 21: Subunit Structure and Covalent Modification. 22: Sequential Processes and Synergistic Effects. PART IV: The Modified Protein: Isolation and Analysis of Structure. 23: Isolation of Modified Proteins. 24: Amino Acid Analysis of Modified Proteins. 25: Identification of Modified Amino Acids by Physical Methods. 26: Chemical Structure of the Modified Group. 27: Primary Structure of the Modified Site. PART V: Physical and Chemical Properties of Modified Amino Acids. 28: Modification Can Change the Charge of the Protein. 29: Modification Can Change the Hydrophobicity of the Protein. 30: Modification Can Influence Protein Conformation, Folding, and Stability. 31: Flexibility and Function. 32: Modification Can Change Ligand Binding. PART VI: Inhibitors and Activators of Cellular Modification Reactions. 33: Enzyme Inhibitors. 34: Enzyme Activators. PART VII: Biological Effects of Covalent Modification. 35: Reversible and Irreversible Modification. 36: General Criteria for the Biological Role of Protein Modifications. 37: Phosphorylation. 38: Protein Ubiquitination. 39: Covalent Attachment of Long Chain Fatty Acids. 40: Glycosylation. 41: Approaches for the Study of Biological Role