ISSN:
1522-9602
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Mathematics
Notes:
Abstract A frequently used measure for the extent of cooperativity in ligand binding by allosteric proteins is the Hill coefficient. Hill coefficients can be measured for steady-state kinetic data and also for transient kinetic data. Here, the relationship between the two types of Hill coefficients is analysed. It is shown that a value of 1 for the ratio of the two Hill coefficients is a test for a concerted ligand-induced transition between two conformations of the protein, in accordance with the Monod-Wyman-Changeux model. A value of 1 for this ratio has recently been observed for a series of chaperonin GroEL mutants suggesting that ATP-induced allosteric transitions in this protein are concerted.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1006/bulm.1999.0150
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