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Characterization of binding interactions by isothermal titration calorimetry

✍ Scribed by Michael L Doyle

Book ID
104362074
Publisher
Elsevier Science
Year
1997
Tongue
English
Weight
656 KB
Volume
8
Category
Article
ISSN
0958-1669

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✦ Synopsis

Isothermal titration calorimetry is a high-accuracy method for measuring binding affinities. Titration calorimetry is a universal method that has broad impact throughout biotechnology. In recent years, microcalorimeters that are capable of characterizing binding interactions of biological macromolecules have become commercially available. Results from these studies are providing new insight into the molecular nature of macromolecular interactions.

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A rigorous method for the least-squares nonlinear regression analysis of displacement isothermal titration calorimetric data is presented. The method can fit the binding isotherm of a ligand which is competitively inhibited in its binding by another bound ligand to a molecule with n identical and in