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

Positive cooperativity in the functioning of molecular chaperone GroEL.

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Institute of Protein Research, Academy of Sciences of Russia, Moscow Region.


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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