Linked Life Data

10517869

Source:http://linkedlifedata.com/resource/pubmed/id/10517869

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1999-12-23
pubmed:abstractText
Although we have a rather elaborate "working-cycle" for the 60 kDa molecular chaperones, which possess a cavity, and are called Anfinsen-cage-type chaperones to emphasize that they provide a closed, protected environment to help the folding of their substrates, our understanding of the molecular mechanism of how these chaperones help protein folding is still incomplete. The present study adds two novel elements to the mechanism of how Anfinsen-cage-type chaperones (members of the 60 kDa chaperone family) aid protein folding. It is proposed that (1) these chaperones do not generally unfold their targets, but by a multidirectional expansion preferentially loosen the tight, inner structure of the collapsed target protein; and (2) during the expansion water molecules enter the hydrophobic core of the target, this percolation being a key step in chaperone action. This study compares this chaperone-percolator model with existing explanations and suggests further experiments to test it. BioEssays 1999;21:959-965.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0265-9247
pubmed:author
pubmed:copyrightInfo
Copyright 1999 John Wiley & Sons, Inc.
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
959-65
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Chaperone-percolator model: a possible molecular mechanism of Anfinsen-cage-type chaperones.
pubmed:affiliation
Department of Medical Chemistry, Semmelweis University, H-1444 Budapest, P.O. Box 260, Hungary. csermely@puskin.sote.hu
pubmed:publicationType
Journal Article