Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010

Ghai, Rajesh, Falconer, Robert J. and Collins, Brett M. (2012) Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010. Journal of Molecular Recognition, 25 1: 32-52.


Author Ghai, Rajesh
Falconer, Robert J.
Collins, Brett M.
Title Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010
Journal name Journal of Molecular Recognition  (ERA 2012 Listed)    (ERA 2010 Rank B)   Check publisher's open access policy
Publication date 2012-01
Sub-type Review of research - research literature review (NOT book review
Year available 2011
DOI 10.1002/jmr.1167
Volume number 25
Issue number 1
ISSN 0952-3499
1099-1352
Start page 32
End page 52
Total pages 21
Place of publication Bognor Regis, West Sussex, United Kingdom
Publisher John Wiley & Sons
Collection year 2012
Language eng
Formatted abstract Isothermal titration calorimetry (ITC) is a biophysical technique for measuring the formation and dissociation of molecular complexes and has become an invaluable tool in many branches of science from cell biology to food chemistry. By measuring the heat absorbed or released during bond formation, ITC provides accurate, rapid, and label-free measurement of the thermodynamics of molecular interactions. In this review, we survey the recent literature reporting the use of ITC and have highlighted a number of interesting studies that provide a flavour of the diverse systems to which ITC can be applied. These include measurements of protein-protein and protein-membrane interactions required for macromolecular assembly, analysis of enzyme kinetics, experimental validation of molecular dynamics simulations, and even in manufacturing applications such as food science. Some highlights include studies of the biological complex formed by Staphylococcus aureus enterotoxin C3 and the murine T-cell receptor, the mechanism of membrane association of the Parkinson's disease-associated protein α-synuclein, and the role of non-specific tannin-protein interactions in the quality of different beverages. Recent developments in automation are overcoming limitations on throughput imposed by previous manual procedures and promise to greatly extend usefulness of ITC in the future. We also attempt to impart some practical advice for getting the most out of ITC data for those researchers less familiar with the method.
Keyword Thermodynamics
Calorimetry
Interactions
Drug discovery
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Article first published online: 29 DEC 2011

Document type: Journal Article
Sub-type: Review of research - research literature review (NOT book review
Collections: Official 2013 Collection
Institute for Molecular Bioscience - Publications
 
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