Analysis of cooperativity by isothermal titration calorimetry

Cooperative binding pervades Nature. This review discusses the use of isothermal titration calorimetry (ITC) in the identification and characterisation of cooperativity in biological interactions. ITC has broad scope in the analysis of cooperativity as it determines binding stiochiometries, affiniti...

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Veröffentlicht in:	International journal of molecular sciences 2009-08, Vol.10 (8), p.3457-3477
1. Verfasser:	Brown, Alan
Format:	Artikel
Sprache:	eng
Schlagworte:	Archaeal Proteins - chemistry Archaeal Proteins - metabolism Calorimetry DNA - chemistry DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Fatty Acid-Binding Proteins - chemistry Fatty Acid-Binding Proteins - metabolism Gastrointestinal Hormones - chemistry Gastrointestinal Hormones - metabolism Humans Kinetics Ligands Magnetic Resonance Spectroscopy Protein Binding Review Thermodynamics Thioredoxin-Disulfide Reductase - chemistry Thioredoxin-Disulfide Reductase - metabolism
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Beschreibung
Zusammenfassung:	Cooperative binding pervades Nature. This review discusses the use of isothermal titration calorimetry (ITC) in the identification and characterisation of cooperativity in biological interactions. ITC has broad scope in the analysis of cooperativity as it determines binding stiochiometries, affinities and thermodynamic parameters, including enthalpy and entropy in a single experiment. Examples from the literature are used to demonstrate the applicability of ITC in the characterisation of cooperative systems.
ISSN:	1422-0067 1661-6596 1422-0067
DOI:	10.3390/ijms10083457