Coupling of protein relaxation to ligand binding and migration in myoglobin

Abstract

Protein relaxation, ligand binding, and ligand migration into a hydrophobia cavity in myoglobin are unified by a bounded diffusion model which produces an accurate fit to complex ligand rebinding data over eight decades in time and a 160 K temperature range, in qualitative agreement with time-resolved x-ray crystallography. Protein relaxation operates in a cyclic manner to move the ligand away from the binding site.