Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy
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We developed a new method to elucidate the binding kinetics k(on) and k(off), and the dissociation constant K(D) (=k(off)/k(on)), of protein-protein interactions without observable bound resonances of the protein of interest due to high molecular weight in a c... ...
