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Volume 272, Number 27, Issue of July 4, 1997 pp. 16737-16740
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Mutants of Rat Intestinal Fatty Acid-binding Protein Illustrate the Critical Role Played by Enthalpy-Entropy Compensation in Ligand Binding

(Received for publication, April 21, 1997, and in revised form, May 2, 1997)

Gary V. Richieri , Pamela J. Low , Ronald T. Ogata and Alan M. Kleinfeld

From the Medical Biology Institute, La Jolla, California 92037

Site-specific variants of rat intestinal fatty acid-binding protein were constructed to identify the molecular interactions that are important for binding to fatty acids (FAs). Several variants displayed affinities that appeared incompatible with the crystal structure of the protein-FA complex. Thermodynamic measurements provided an explanation for these apparent inconsistencies and revealed that binding affinities often inaccurately reported changes in protein-FA interactions because changes in the binding entropy and enthalpy were usually compensatory. These results demonstrate that understanding the effects of amino acid replacements on ligand binding requires measurements of enthalpy and entropy, in addition to affinity.


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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.