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. 1992 Apr 5;267(10):6796-800.

Positive cooperativity in the functioning of molecular chaperone GroEL

E S Bochkareva  1 , N M Lissin, G C Flynn, J E Rothman, A S Girshovich
Affiliations
  • PMID: 1348056
Free article

Positive cooperativity in the functioning of molecular chaperone GroEL

E S Bochkareva et al. J Biol Chem. .
Free article

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.

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