Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins.

Abstract:

:Newly solved chaperone structures include the thermosome, a group II chaperonin, and a small heat-shock protein. Novel ideas on chaperone mechanism are presented in the forced unfolding hypothesis of GroEL action. Structures of chaperone-pilin complexes reveal the mechanism of chaperone interaction in bacterial pilus assembly and there have been major advances in understanding the structure and function of Hsp100 unfoldases.

journal_name

Curr Opin Struct Biol

authors

Saibil H

doi

10.1016/s0959-440x(00)00074-9

subject

Has Abstract

pub_date

2000-04-01 00:00:00

pages

251-8

issue

2

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(00)00074-9

journal_volume

10

pub_type

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