Biophysical Chemistry

Edited by: Neeraja Sankaran THERMODYNAMICS TACTICS: Ruth Spolar and M. Thomas Record postulate that conformational changes occur at the binding interface between proteins and their ligands, accounting for changes in heat capacity and entropoy in these reactions. R.S. Spolar, M.T. Record, Jr., "Coupling of local folding to site-specific binding of proteins to DNA," Science, 263:777-84, 1994. (Cited in 41 publications through April 1994) Comments by Ruth Saecker Spolar, department of chemistry,

The Scientist Staff
May 28, 1995

Edited by: Neeraja Sankaran


THERMODYNAMICS TACTICS: Ruth Spolar and M. Thomas Record postulate that conformational changes occur at the binding interface between proteins and their ligands, accounting for changes in heat capacity and entropoy in these reactions.
R.S. Spolar, M.T. Record, Jr., "Coupling of local folding to site-specific binding of proteins to DNA," Science, 263:777-84, 1994. (Cited in 41 publications through April 1994)

Comments by Ruth Saecker Spolar, department of chemistry, and M. Thomas Record, Jr., department of biochemistry, University of Wisconsin, Madison

The underlying theme of this paper, according to its authors, is that it provides a basis for understanding the stability and specificity of interactions of proteins with other proteins, nucleic acids, and ligands in thermodynamic terms. They speculate that this approach may be of interest because of its use in relating the molecular structure with function and explaining molecular-recognition events.

"Our focus has been...

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