Guidebook to Molecular Chaperones and Protein-Folding Catalysts [Paperback]

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.

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

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. OthlS`