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On the Relationship Between the Hill Coefficients for Steady-state and Transient Kinetic Data: A Criterion for Concerted Transitions in Allosteric Proteins

✍ Scribed by Amnon Horovitz; Ofer Yifrach


Publisher
Springer
Year
2000
Tongue
English
Weight
61 KB
Volume
62
Category
Article
ISSN
1522-9602

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✦ Synopsis


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.