Determination of the Kinetics and Thermodynamics of Ligand Binding to a Specific Inactive Conformation in Protein Kinases
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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.
Key wordsKinase Inactive conformation DFG-out Activation loop Fluorescent probe Protein ligand Dissociation constant
This work was supported by the National Institute of General Medical Science (R01GM086858).