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Curr Opin Biotechnol. 1994 Aug;5(4):381-8.

Acquisition and use of calorimetric data for prediction of the thermodynamics of ligand-binding and folding reactions of proteins.

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Vertex Pharmaceuticals Inc, Cambridge.


The commercialization of high-precision microcalorimeters has led to a sharp increase in the acquisition and utilization of calorimetric data on the binding and folding reactions of proteins. This thermodynamic database, together with high-resolution structures of proteins and their complexes with ligands, has facilitated the development, calibration, refinement and testing of empirically based and computational methods for predicting the thermodynamics of processes involving macromolecules. Even so, a generally accepted method for assigning structural parameters to the various energetic contributions of protein folding and ligand-binding reactions, much less a method for predicting the changes in thermodynamic parameters of these reactions, has not yet been firmly established.

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