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Guidebook to Molecular Chaperones and Protein-Folding Catalysts

Series: Sambrook and Tooze Guidebook Series

Edited By: Mary-Jane Gething

Oxford University Press

Paperback | Nov 1997 | #84065 | ISBN: 019859948X
Availability: Usually dispatched within 2-3 weeks Details
NHBS Price: £69.99 $92/€79 approx
Hardback | Dec 1997 | #84064 | ISBN: 0198599498
Out of Print Details

About this book

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.

"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. 4 Stars." --Doody's Journal

"The book is divided into 17 parts, with the first 15 cataloguing the different classes of molecular chaperones. Information on nearly 200 chaperones have been included. Each part contains a brief entry, typically between one to three pages in length, of each family member. In the literature, many chaperones are referred to by more than one name, and a particularly useful feature in the book is the listing of these alternative names. Other information includes isolation, gene sequence, biological activities, regulation, biolo


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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