UNSPECIFIED. (1994) ROLES OF MOLECULAR CHAPERONES IN PROTEIN-FOLDING. CURRENT OPINION IN STRUCTURAL BIOLOGY, 4 (1). pp. 117-122. ISSN 0959-440X

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.

Data sourced from Thomson Reuters' Web of Knowledge

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