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Table of contents
- Contentsvii
- Contributorsxi
- Prefacexiii
- Chapter 1. Chaperonins: Introductory Perspective1
- I. Origins2
- II. General Concept of Molecular Chaperones8
- III. Definitions and Nomenclature12
- IV. Functions of Chaperonins15
- V. Problems17
- References23
- Chapter 2. Evolutionary Relationships of Chaperonins27
- I. Introduction27
- II. Chaperonin 60 and Chaperonin 10 Gene Families28
- III. t-Complex Polypeptide 1 Gene Family47
- IV. Evolutionary Relationship of t-Complex Polypeptide 1 and Chaperonin 60 Gene Families and Origin52
- References57
- Chapter 3. Chaperonins of Photosynthetic Organisms65
- I. Introduction65
- II. Chloroplast Chaperonins68
- III. Chaperonin 60 and Chaperonin 10 in Mitochondria from Angiosperms79
- IV. Chaperonin 60 and Chaperonin 10 in Photosynthetic Prokaryotic Organisms81
- V. Concluding Comments83
- References85
- Chapter 4. Chaperonin-Mediated Folding and Assembly of Proteins in Mitochondria91
- I. Introduction91
- II. Mitochondrial Chaperonin 6093
- III. Mitochondrial Chaperonin 60 as Stress Protein96
- IV. Regulation of Mitochondrial Chaperonin 60 Function by Mitochondrial Chaperonin 1097
- V. Role of Mitochondrial Chaperonin 60 Machinery in Intramitochondrial Protein Sorting99
- VI. Cooperation of Mitochondrial Chaperonin 60 with Mitochondrial Heat Shock Protein 70 Machinery100
- VII. Perspectives102
- References103
- Chapter 5. Structure and Function of Chaperonins in Archaebacteria and Eukaryotic Cytosol107
- I. Introduction108
- II. Archaebacterial Chaperonins110
- III. t-Complex Polypeptide 1 in Eukaryotic Cytosol113
- IV. CCT Analysis in Yeast125
- V. Evolution127
- VI. Conclusions130
- References131
- Chapter 6. Regulation of Chaperonin Gene Expression137
- I. Introduction137
- II. Chaperonin Gene Organization138
- III. Induction of Chaperonin Synthesis in Response to Stress143
- IV. Regulation of Escherichia coli Chaperonin Genes144
- V. Regulation of Chaperonin Genes in Other Bacteria, Including Gram- Positive Bacteria150
- VI. Modulation of Chaperonin Activity by Bacteriophage Gp31 Protein159
- VII. Concluding Remarks160
- References161
- Chapter 7. Kinetic and Energetic Aspects of Chaperonin Function167
- I. Ground Rules of Chaperonin Behavior168
- II. Avoidance of Dead Ends180
- III. Spontaneous Protein Folding182
- IV. Energy Transduction: Role of ATP in Chaperonin Activity184
- V. Conformation of Bound Protein Substrates195
- VI. General Models of Chaperonin Action200
- References208
- Chapter 8. Role of Prokaryotic Chaperonins in Protein Folding213
- I. Introduction213
- II. Pathway of Chaperone-Assisted Protein Folding217
- III. Mechanism of Chaperonin-Mediated Protein Folding221
- IV. Conformational Properties of Chaperonin-Bound Proteins229
- V. Role of Chaperonins in Oligomeric Protein Assembly233
- VI. Chaperonin Function under Cellular Stress Conditions234
- VII. Concluding Remarks237
- References237
- Chapter 9. Chaperonin Structure and Conformational Changes245
- I. Introduction: Methods for Structural Studies of Chaperonins246
- II. Arrangement of Subunit Domains in Chaperonin 60 Oligomer249
- III. Crystal Structures of GroEL and GroES251
- IV. Conformational Changes in GroEL and Its Complexes Studied by Cryoelectron Microscopy258
- V. Molecular Basis of Chaperonin Function261
- References263
- Chapter 10. Immunological Aspects of Chaperonins267
- I. Innate Immunity: Direct Effect of Chaperonins on Phagocytes268
- II. Adaptive Immunity: Nature of Immune Response to Chaperonins273
- III. Significance of Immune Response282
- IV. Conclusion288
- References289
- Index297
- Color Plate Section322
Book details
- Vendor Elsevier S & T
- SKU 9780122374555
- ISBN-13 9780080528885
- Author Ellis, Robert L.
- Category Science
- Subject Biotechnology
Do you have questions about this book?
The first of its kind, this volume presents the latest research findings on the chaperonins, the best studied family of a class of proteins known as molecular chaperones. These findings are changing our view of some fundamental cellular processes involving proteins, especially how proteins fold into their functional conformations.
Key Features
* Origins of the new view of protein folding
* Prokaryotic chaperonins
* Eukaryotic chaperonins
* Evolution of the chaperonins
* Refolding of denatured proteins
* Organelle biosynthesis
* Biomedical aspects
Key Features
* Origins of the new view of protein folding
* Prokaryotic chaperonins
* Eukaryotic chaperonins
* Evolution of the chaperonins
* Refolding of denatured proteins
* Organelle biosynthesis
* Biomedical aspects
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