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Originally published as Biophys J. BioFAST on April 15, 2005.
doi:10.1529/biophysj.105.060194
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Biophysical Journal 89:76-79 (2005)
© 2005 The Biophysical Society

An Empirical Extremum Principle for the Hill Coefficient in Ligand-Protein Interactions Showing Negative Cooperativity

Hagai Abeliovich

Department of Biochemistry and Food Science, Hebrew University of Jerusalem, Rehovot, Israel

Correspondence: Address reprint requests to H. Abeliovich, Dept. of Biochemistry and Food Science, Hebrew University of Jerusalem, Rehovot, Israel 76100. Tel.: 972-8-948-9060; E-mail: ahagai{at}agri.huji.ac.il.

The Hill coefficient (nH) is a central parameter in the study of ligand-protein interactions, which measures the degree of cooperativity between subunits that bind the ligand in multisubunit proteins. The most common usage of nH is as an estimate of the minimal number of interacting binding sites in positively cooperating systems. In the present study, a statistical interpretation of nH for a generalized system of multiple identical binding sites is developed. This interpretation is then applied to the derivation of an empirical extremum principle for nH in negatively cooperating systems of identical binding sites, which can be used for the estimation of the minimal number of interacting sites in such systems.




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