Guidebook to Molecular Chaperones and Protein-Folding Catalysts

Overview


The precise shape of a protein is a crucial factor in its function. How do proteins become folded into the right conformation? Molecular chaperones and protein folding catalysts bind to developing polypeptides in the cytoplasm and ensure correct folding and transport. This Guidebook catalogues the latest information on nearly 200 of these molecules, including the important class of heat shock proteins; each entry is written by leading researchers in the field.

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Overview


The precise shape of a protein is a crucial factor in its function. How do proteins become folded into the right conformation? Molecular chaperones and protein folding catalysts bind to developing polypeptides in the cytoplasm and ensure correct folding and transport. This Guidebook catalogues the latest information on nearly 200 of these molecules, including the important class of heat shock proteins; each entry is written by leading researchers in the field.

The book contains black-and-white illustrations.

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Editorial Reviews

Doody's Review Service
Reviewer: Fulong Tan, PhD (University of Illinois at Chicago College of Medicine)
Description: This book, one in the Guidebook series, is a comprehensive guide to the structure and function of proteins involved in polypeptide folding.
Purpose: Recently gained knowledge in protein folding is so vast that even specialists find it difficult to keep up. The purpose of this book is to provide readers with a compendium of current knowledge about chaperones and folding catalysts. This is a worthy objective, as I have not seen a similar book, and the book achieves its goal.
Audience: The book is meant to provide an overview for researchers in the protein folding field (e.g., graduate students, postdoctoral fellows, principal investigators), and to help newcomers gain access to unfamiliar work rapidly. The book achieves its purpose and is appropriately targeted.
Features: The illustrations are adequate in number and of high quality. The bibliographies are concise and the references are relatively current. Other helpful features include: an overall list of abbreviations; a short abstract for each entry; an overview chapter for each protein family; GenBank accession numbers; and alternative names for the proteins. All of these features help readers to rapidly access needed information .
Assessment: This book describes important aspects of the structure, function, and regulation of all known chaperones and enzymes involved in protein folding. The information is up-to-date and the text is arranged in a concise and easy to read format. This is a useful handbook, not only for scientists in the protein folding field, but also for those working in related areas for whom the comprehensive summaries will be especially valuable. As a reference book in health science libraries, it will help newcomers become familiar with the field and rapidly find needed information.
Fulong Tan
This book, one in the Guidebook series, is a comprehensive guide to the structure and function of proteins involved in polypeptide folding. Recently gained knowledge in protein folding is so vast that even specialists find it difficult to keep up. The purpose of this book is to provide readers with a compendium of current knowledge about chaperones and folding catalysts. This is a worthy objective, as I have not seen a similar book, and the book achieves its goal. The book is meant to provide an overview for researchers in the protein folding field (e.g., graduate students, postdoctoral fellows, principal investigators), and to help newcomers gain access to unfamiliar work rapidly. The book achieves its purpose and is appropriately targeted. The illustrations are adequate in number and of high quality. The bibliographies are concise and the references are relatively current. Other helpful features include: an overall list of abbreviations; a short abstract for each entry; an overview chapter for each protein family; GenBank accession numbers; and alternative names for the proteins. All of these features help readers to rapidly access needed information . This book describes important aspects of the structure, function, and regulation of all known chaperones and enzymes involved in protein folding. The information is up-to-date and the text is arranged in a concise and easy to read format. This is a useful handbook, not only for scientists in the protein folding field, but also for those working in related areas for whom the comprehensive summaries will be especially valuable. As a reference book in health science libraries, it will help newcomers become familiar with the fieldand rapidly find needed information.

4 Stars! from Doody
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Product Details

  • ISBN-13: 9780198599494
  • Publisher: A Sambrook and Tooze Publication at Oxford University Press
  • Publication date: 1/28/1997
  • Series: Guidebook Series
  • Edition number: 1
  • Pages: 584
  • Product dimensions: 7.70 (w) x 9.80 (h) x 1.50 (d)

Table of Contents

1. HSP70 proteins
2. HSP110/SSE proteins
3. HSP40 (DNAJ-related) proteins
4. GRPE-like proteins
5. HSP90 proteins
6. CPN60 and CPN10 proteins
7. Cytosolic chaperonins
8. HSP100 proteins
9. Small HSPs
10. Calnexin and calreticulin
11. PDI and thioredoxin-related proteins
12. Peptidyl-prolyl isomerases
12A. Cyclophilin PPIases
12B. FK-506 binding proteins
12C. Parvulin PP1ases
13. Individual chaperonins
14. Protein specific chaperones
15. Intramolecular chaperones
16. Molecular chaperone machine
17. Cellular regulation of chaperone activity

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