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.
Original language | English |
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Pages (from-to) | 1537-1543 |
Number of pages | 7 |
Journal | Biophysical Journal |
Volume | 87 |
Issue number | 3 |
DOIs | |
State | Published - Sep 2004 |