Applications of isothermal titration calorimetry in protein science
Yi Liang,
Corresponding Author
Yi Liang
State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China
*Corresponding author: Tel/Fax, 86-27-68754902; E-mail, [email protected]Search for more papers by this authorYi Liang,
Corresponding Author
Yi Liang
State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China
*Corresponding author: Tel/Fax, 86-27-68754902; E-mail, [email protected]Search for more papers by this authorThis work was supported by grants from the National Key Basic Research Foundation of China (No. 2006CB910301), the National Natural Science Foundation of China (No. 30770421) and the Program for New Century Excellent Talents in University (No. NCET-04-0670)
Abstract
During the past decade, isothermal titration calorimetry (ITC) has developed from a specialist method for understanding molecular interactions and other biological processes within cells to a more robust, widely used method. Nowadays, ITC is used to investigate all types of protein interactions, including protein-protein interactions, protein-DNA/RNA interactions, protein-small molecule interactions and enzyme kinetics; it provides a direct route to the complete thermodynamic characterization of protein interactions. This review concentrates on the new applications of ITC in protein folding and misfolding, its traditional application in protein interactions, and an overview of what can be achieved in the field of protein science using this method and what developments are likely to occur in the near future. Also, this review discusses some new developments of ITC method in protein science, such as the reverse titration of ITC and the displacement method of ITC.
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