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
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description 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.
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subjects 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
title Analysis of cooperativity by isothermal titration calorimetry
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