Abstract
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.
Keywords:
NMR; cooperativity; global analysis; isothermal titration calorimetry; multiprotein complexes; stoichiometry; thermodynamics.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Archaeal Proteins / chemistry
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Archaeal Proteins / metabolism
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Calorimetry*
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DNA / chemistry
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DNA / metabolism
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / metabolism
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Fatty Acid-Binding Proteins / chemistry
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Fatty Acid-Binding Proteins / metabolism
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Gastrointestinal Hormones / chemistry
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Gastrointestinal Hormones / metabolism
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Humans
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Kinetics
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Ligands*
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Magnetic Resonance Spectroscopy
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Protein Binding
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Thermodynamics
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Thioredoxin-Disulfide Reductase / chemistry
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Thioredoxin-Disulfide Reductase / metabolism
Substances
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Archaeal Proteins
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DNA-Binding Proteins
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Fatty Acid-Binding Proteins
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Gastrointestinal Hormones
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Ligands
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fatty acid-binding protein 6
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Sac7 protein, Sulfolobus
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DNA
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Thioredoxin-Disulfide Reductase