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.
Product Details
84075
9780198599487
9780198599487
Data sheet
Publication date
1997
Issue number
1
Cover
paperback
Pages count
580
Dimensions (mm)
188 x 246
Weight (g)
1276
HSP70 proteins; HSP110/SSE proteins; HSP40 (DNAJ-related) proteins; GRPE-like proteins; HSP90 proteins; CPN60 and CPN10 proteins; Cytosolic chaperonins; HSP100 proteins; Small HSPs; Calnexin and calreticulin; PDI and thioredoxin-related proteins; Peptidyl-prolyl isomerases; Cyclophilin PPIases; FK-506 binding proteins; Parvulin PP1ases; Individual chaperonins; Protein specific chaperones; Intramolecular chaperones; Molecular chaperone machine; Cellular regulation of chaperone activity;
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