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Positive cooperativity in the functioning of molecular chaperone GroEL
E S Bochkareva1, N M Lissin, G C Flynn
1Institute of Protein Research, Academy of Sciences of Russia, Moscow Region.
The Journal of Biological Chemistry
|April 5, 1992
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.