Guidebook to Molecular Chaperones and Protein-Folding Catalysts

Paperback | August 1, 1997

EditorMary-Jane Gething

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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 cataloguesthe 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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From the Publisher

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 cataloguesthe latest information on nearly 200 of the...

Dr Mary-Jane Gething (Partner in the Sambrook and Tooze Partnership, our co-publishers of the Guidebooks Series) Dept of Biochemistry, Melbourne University, Parkville 3052, Australia. Tel: 00 61 3 9344 5948. Fax: 00613 9347 9109. Email: gething@ariel.ucs.unimelb.edu.au
Format:PaperbackDimensions:580 pages, 9.69 × 7.44 × 1.34 inPublished:August 1, 1997Publisher:Oxford University Press

The following ISBNs are associated with this title:

ISBN - 10:019859948X

ISBN - 13:9780198599487

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Table of Contents

1. HSP70 proteins2. HSP110/SSE proteins3. HSP40 (DNAJ-related) proteins4. GRPE-like proteins5. HSP90 proteins6. CPN60 and CPN10 proteins7. Cytosolic chaperonins8. HSP100 proteins9. Small HSPs10. Calnexin and calreticulin11. PDI and thioredoxin-related proteins12. Peptidyl-prolyl isomerases12A. Cyclophilin PPIases12B. FK-506 binding proteins12C. Parvulin PP1ases13. Individual chaperonins14. Protein specific chaperones15. Intramolecular chaperones16. Molecular chaperone machine17. Cellular regulation of chaperone activity

Editorial Reviews

"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 theprotein 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, manychaperones 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, biological interactions and mutagenesis studies. . . . ÝT¨he book is amust for everyone working in the field of molecular chaperones. In addition, since protein folding is an integral part of the general field of protein science, it will also be invaluable to anyone interested in that field. The book should be on the shelf of every library housing biologically andbiochemically relevant literature."--The Quarterly Review of Biology