On the relationship between the Hill coefficients for steady-state and transient kinetic data: a criterion for concerted transitions in allosteric proteins.
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.
Horovitz
A
A
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Yifrach
O
O
D000495:Allosteric Site; D018834:Chaperonin 60 / Q000737:chemistry*; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical
D018834:Chaperonin 60; D008024:Ligands