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Coupling of Protein Relaxation to Ligand Binding and Migration in Myoglobin

Department of Physical Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel

Correspondence: Address reprint requests to Noam Agmon, E-mail: agmon{at}fh.huji.ac.il.

Protein relaxation, ligand binding, and ligand migration into a hydrophobic 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.

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