Determination of the kinetics and thermodynamics of ligand binding to a specific inactive conformation in protein kinases.

Abstract

Recent interest in inactive kinase conformations has generated the need to develop new biochemical tools to study them. Here, we describe the use of a fluorescent probe that selectively and potently binds to a specific inactive conformation of protein kinases. This allows for the thermodynamics and kinetics of ligand binding to be determined. 
DOI: 10.1007/978-1-62703-008-3_12

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Cite this paper

@article{Hari2012DeterminationOT, title={Determination of the kinetics and thermodynamics of ligand binding to a specific inactive conformation in protein kinases.}, author={Sanjay B. Hari and Pratistha Ranjitkar and Dustin J Maly}, journal={Methods in molecular biology}, year={2012}, volume={928}, pages={153-9} }