Applications of calorimetric methods to drug discovery and the study of protein interactions

Recent studies report the application of isothermal titration calorimetry and differential scanning calorimetry to the study of protein–ligand interactions, allosteric cooperativity and aspects of protein folding. New methods of data analysis compare alternative methods for determining ligand bindin...

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Bibliographic Details
Published inCurrent opinion in structural biology Vol. 13; no. 1; pp. 115 - 121
Main Authors Weber, Patricia C, Salemme, F Raymond
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.02.2003
Subjects
Calorimetry - instrumentation
Calorimetry - methods
Calorimetry, Differential Scanning - instrumentation
Calorimetry, Differential Scanning - methods
Drug Design
Energy Transfer
Entropy
Ligands
Macromolecular Substances
Protein Binding
Protein Conformation
Protein Denaturation
Protein Structure, Tertiary
Proteins - chemistry
Temperature
DNSA
ITC
CBS
DSC
RalGDS
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Summary:Recent studies report the application of isothermal titration calorimetry and differential scanning calorimetry to the study of protein–ligand 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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
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ObjectType-Review-1
ISSN:0959-440X
1879-033X
DOI:10.1016/S0959-440X(03)00003-4