ROLES OF MOLECULAR CHAPERONES IN PROTEIN-FOLDING
UNSPECIFIED (1994) ROLES OF MOLECULAR CHAPERONES IN PROTEIN-FOLDING. CURRENT OPINION IN STRUCTURAL BIOLOGY, 4 (1). pp. 117-122. ISSN 0959-440XFull text not available from this repository.
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|
|Number of Pages:||6|
|Page Range:||pp. 117-122|
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