PMID: 6108194Jan 1, 1980Paper

The thermodynamics of nucleotide binding to proteins

CRC Critical Reviews in Biochemistry
N V Beaudette, N Langerman

Abstract

Models describing the interaction of a small molecule with a protein are typically couched in terms of the stoichiometry, cooperativity, and binding free-energy change. These parameters are readily available from equilibrium dialysis experiments (or appropriate variations). With the recent advent of extremely sensitive calorimeters, it is possible to obtain thermal data for the binding reaction and, thus, the entire set of thermodynamic parameters, delta G', delta H', delta S', delta C', become readily available. This review is limited to the binding of nucleotides and nucleotide analogs to proteins for which complete thermal data are available. While the majority of such systems have been characterized by calorimetry, we have not excluded, per se, van't Hoff enthalpy determinations. The systems we have considered include, but are not limited to, thymidylate synthetase, phosphorylase, several dehydrogenases, aldolase, glutamine synthetase, hemoglobin, asparate transcarbamylase, and ribonuclease. A variety of forces contribute to the total free-energy change upon ligand binding. These forces include ionic, van der Waals, hydrogen bond, and hydrophobic. In several cases, properly designed experiments have allowed a partial resolu...Continue Reading

References

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Citations

Nov 28, 2007·Nucleic Acids Research·Marie F SoulièreMartin Bisaillon
Mar 1, 1982·Archives of Biochemistry and Biophysics·H P Nowak, N Langerman
Jan 18, 2006·FEBS Letters·Ines BenzaghouMartin Bisaillon
Aug 17, 2004·The Biochemical Journal·Isabelle BougieMartin Bisaillon
Oct 3, 2001·The Journal of Biological Chemistry·G M WilsonG Brewer
Jun 2, 1998·Archives of Biochemistry and Biophysics·S NarasimhuluJ D Winkler

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