Format

Send to

Choose Destination
Curr Opin Struct Biol. 1997 Feb;7(1):41-52.

Chaperone-assisted protein folding.

Author information

1
Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Box G-J2, Providence, RI 02912, USA.

Abstract

Molecular chaperones of the Hsp70 and chaperonin families are basic constituents of the cellular machinery that mediates protein folding. Recent functional and structural studies corroborate existing models for the mechanism of these components. Highlights of the past year include the X-ray crystallographic analysis of the peptide-binding domain of the Escherichia coli Hsp70 homolog, DnaK, the direct demonstration of protein folding in the central cavity of the chaperonin GroEL, and the visualization of conformational changes in GroEL during the chaperonin folding cycle.

PMID:
9032064
DOI:
10.1016/s0959-440x(97)80006-1
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center