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To determine inhibition constant (Ki) of tight-binding inhibitor, the putative method estimated an apparent Ki from the response of initial rates to total concentrations of the inhibitor considering its depletion during binding for conversion into the true Ki, but was impractical with glutathione S-transferase of sophisticated kinetics. A fluorometric titration assay of dissociation constant (K...
Homogenous bioaffinity analysis with tryptophan/tyrosine residues in native proteins as FÖrster-resonance-energy-transfer (FRET) donors is feasible when suitable fluorophors can act as FRET acceptors in ligands (FRET probes) and FRET efficiency in complexes of proteins and FRET probes is high enough. In complexes of proteins and FRET probes, suitable acceptors should have excitation peaks around 335 nm...
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