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The chaperonins / edited by R. John Ellis.

EBSCOhost Academic eBook Collection (North America) Available online

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eBook EngineeringCore Collection Available online

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Format:
Book
Contributor:
Ellis, R. J. (Reginald John), 1935- editor.
Hartl, F. Ulrich MSKCC
Mayhew, Mark N. MSKCC.
Memorial Sloan Kettering Cancer Center (MSKCC).
Series:
Cell biology.
Cell biology
Language:
English
Subjects (All):
Molecular chaperones.
Physical Description:
1 online resource (339 p.)
Place of Publication:
San Diego, California : Academic Press, 1996.
Language Note:
English
Summary:
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
Contents:
Front Cover; The Chaperonins; Copyright Page; Contents; Contributors; Preface; Chapter 1. Chaperonins: Introductory Perspective; I. Origins; II. General Concept of Molecular Chaperones; III. Definitions and Nomenclature; IV. Functions of Chaperonins; V. Problems; References; Chapter 2. Evolutionary Relationships of Chaperonins; I. Introduction; II. Chaperonin 60 and Chaperonin 10 Gene Families; III. t-Complex Polypeptide 1 Gene Family; IV. Evolutionary Relationship of t-Complex Polypeptide 1 and Chaperonin 60 Gene Families and Origin of Eukaryotic Cells; References
Chapter 3. Chaperonins of Photosynthetic OrganismsI. Introduction; II. Chloroplast Chaperonins; III. Chaperonin 60 and Chaperonin 10 in Mitochondria from Angiosperms; IV. Chaperonin 60 and Chaperonin 10 in Photosynthetic Prokaryotic Organisms; V. Concluding Comments; References; Chapter 4. Chaperonin-Mediated Folding and Assembly of Proteins in Mitochondria; I. Introduction; II. Mitochondrial Chaperonin 60; III. Mitochondrial Chaperonin 60 as Stress Protein; IV. Regulation of Mitochondrial Chaperonin 60 Function by Mitochondrial Chaperonin 10
V. Role of Mitochondrial Chaperonin 60 Machinery in Intramitochondrial Protein SortingVI. Cooperation of Mitochondrial Chaperonin 60 with Mitochondrial Heat Shock Protein 70 Machinery; VII. Perspectives; References; Chapter 5. Structure and Function of Chaperonins in Archaebacteria and Eukaryotic Cytosol; I. Introduction; II. Archaebacterial Chaperonins; III. t-Complex Polypeptide 1 in Eukaryotic Cytosol; IV. CCT Analysis in Yeast; V. Evolution; VI. Conclusions; References; Chapter 6. Regulation of Chaperonin Gene Expression; I. Introduction; II. Chaperonin Gene Organization
III. Induction of Chaperonin Synthesis in Response to StressIV. Regulation of Escherichia coli Chaperonin Genes; V. Regulation of Chaperonin Genes in Other Bacteria, Including Gram- Positive Bacteria; VI. Modulation of Chaperonin Activity by Bacteriophage Gp31 Protein; VII. Concluding Remarks; References; Chapter 7. Kinetic and Energetic Aspects of Chaperonin Function; I. Ground Rules of Chaperonin Behavior; II. Avoidance of Dead Ends; III. Spontaneous Protein Folding; IV. Energy Transduction: Role of ATP in Chaperonin Activity; V. Conformation of Bound Protein Substrates
VI. General Models of Chaperonin ActionReferences; Chapter 8. Role of Prokaryotic Chaperonins in Protein Folding; I. Introduction; II. Pathway of Chaperone-Assisted Protein Folding; III. Mechanism of Chaperonin-Mediated Protein Folding; IV. Conformational Properties of Chaperonin-Bound Proteins; V. Role of Chaperonins in Oligomeric Protein Assembly; VI. Chaperonin Function under Cellular Stress Conditions; VII. Concluding Remarks; References; Chapter 9. Chaperonin Structure and Conformational Changes; I. Introduction: Methods for Structural Studies of Chaperonins
II. Arrangement of Subunit Domains in Chaperonin 60 Oligomer
Notes:
Description based upon print version of record.
Includes bibliographical references at the end of each chapters and index.
Description based on print version record.
ISBN:
1-281-04644-2
9786611046446
0-08-052888-0
OCLC:
476104129

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