Positive cooperativity in the functioning of molecular chaperone GroEL Journal Article


Authors: Bochkareva, E. S.; Lissin, N. M.; Flynn, G. C.; Rothman, J. E.; Girshovich, A. S.
Article Title: Positive cooperativity in the functioning of molecular chaperone GroEL
Abstract: In the presence of its partner, GroES, the tetradecameric molecular chaperone GroEL binds 14 ATP molecules, half of which are hydrolyzed in a cooperative manner. Moreover GroEL can bind, with a positive cooperativity, more than two molecules of nonfolded protein rhodanese. The role of the cooperative mechanism in the functioning of GroEL is discussed.
Keywords: protein; atp hydrolysis; association; escherichia-coli; purification; carboxylase; denatured rhodanese
Journal Title: Journal of Biological Chemistry
Volume: 267
Issue: 10
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 1992-04-05
Start Page: 6796
End Page: 6800
Language: English
ACCESSION: WOS:A1992HM05300052
PROVIDER: wos
PUBMED: 1348056
Notes: Article -- Source: Wos
Citation Impact
MSK Authors
  1. James E Rothman
    120 Rothman