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ROLES OF MOLECULAR CHAPERONES IN PROTEIN-FOLDING

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UNSPECIFIED (1994) ROLES OF MOLECULAR CHAPERONES IN PROTEIN-FOLDING. CURRENT OPINION IN STRUCTURAL BIOLOGY, 4 (1). pp. 117-122.

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Abstract

The idea that in living cells, proteins fold spontaneously in an energy-independent fashion, as they can in vitro, is being replaced by the concept that protein folding in vivo is assisted by pre-existing proteins called molecular chaperones, some of which hydrolyse ATP. The mechanism of action of some of these molecular chaperones has recently been better defined, and confirms the view that they act not by providing steric information but by minimizing the formation of misfolded structures.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Journal or Publication Title: CURRENT OPINION IN STRUCTURAL BIOLOGY
Publisher: CURRENT BIOLOGY LTD
ISSN: 0959-440X
Official Date: February 1994
Dates:
DateEvent
February 1994UNSPECIFIED
Volume: 4
Number: 1
Number of Pages: 6
Page Range: pp. 117-122
Publication Status: Published

Data sourced from Thomson Reuters' Web of Knowledge

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