Applications of Isothermal Titration Calorimetry in Protein-ligand Interactions

doi:10.13560/j.cnki.biotech.bull.1985.2017.05.006

Abstract

Abstract: Isothermal titration calorimetry（ITC）is a biophysical technique widely used to study molecular interactions in molecular biology and these related fields,it is the sole direct method to measure the heat change during complex formation at constant temperature. We may obtain much important information about molecular interactions（such as binding constant,number of binding sites,free energy,enthalpy,and entropy）simply by measuring the heat absorbed or released during an interaction between two liquid solutions. This review concentrates on the principle and features of ITC,the new applications of ITC in protein-ligand interactions,and potential development direction,it has been shown that it plays an important role in the elucidation of binding mechanisms and the validity of the data.

Key words: isothermal titration calorimetry, thermodynamics, interaction, protein, small molecule

QI Xin-jie, WANG Yue, WANG Yan-sheng, FANG Guo-kang, HUANG Ying-chun. Applications of Isothermal Titration Calorimetry in Protein-ligand Interactions[J]. Biotechnology Bulletin, 2017, 33(5): 40-49.

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