Selective control of ligand binding through a distal mutation that alters the protein native ensemble.

Abstract excerpt

Unraveling the molecular mechanisms underlying long-range mutational effects on function is a challenging prospect. In this study, we delineate the consequences of a mutation located at a site distal to the functional region in a promiscuous acyl-CoA binding domain. A W86A mutation at a distal C-terminal segment induces two-stage noncooperative unfolding in an otherwise cooperatively unfolding protein, with the...

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