| Literature DB >> 1683631 |
Abstract
The kinetics of ATP hydrolysis by the 'molecular chaperone' GroEL and the inhibition of this hydrolysis by GroES have been studied in more detail. It is shown that the hydrolysis of ATP by GroEL is cooperative with respect to ATP with a Hill coefficient of 1.86 (+/- 0.13). In the presence of GroES, there is an increase in the degree of cooperativity with a Hill coefficient of 3.01 (+/- 0.18). The observed cooperativity is not due to dissociation of the GroEL oligomer into smaller units but more probably involves structural changes within the GroEL oligomer.Entities:
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Year: 1991 PMID： 1683631 DOI： 10.1016/0014-5793(91)80878-7
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124