Applications of calorimetric methods to drug discovery and the study of protein interactions - Analytical Methods & Tools for Lyophilization

Applications of calorimetric methods to drug discovery and the study of protein interactions
Available online 20 January 2003.
Patricia C Weber and F Raymond Salemme
Current Opinion in Structural Biology
Volume 13, Issue 1 , February 2003
ScienceDirect
3-Dimensional Pharmaceuticals Inc, 1020 Stony Hill Road, Yardley, PA 19067, USA
Abstract
Recent studies report the application of isothermal titration calorimetry and differential scanning calorimetry to the study of proteinÒligand interactions, allosteric cooperativity and aspects of protein folding. New methods of data analysis compare alternative methods for determining ligand binding enthalpy and analyze potential sources of error in the experimental measurement of other thermodynamic parameters. Several reports examine issues concerning drug design and the correlation of thermodynamic and X-ray structural data. New instruments allow volumetric effects in biochemical systems to be evaluated calorimetrically and to substantially expand the throughput of differential scanning calorimetry measurements in drug discovery and other high-throughput applications.
Abbreviations: CBS, 4-carboxybenzenesulfonamide; DNSA, 5-dimethyl-amino-1-naphthalene-sulfonamide; DSC, differential scanning calorimetry; ITC, isothermal titration calorimetry; RalGDS, Ral guanine nucleotide dissociation stimulator
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