Coupling of protein relaxation to ligand binding and migration in myoglobin.
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.
Agmon
Noam
N
Department of Physical Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel. agmon@fh.huji.ac.il
D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D002248:Carbon Monoxide / Q000737:chemistry; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D004058:Diffusion; D005990:Glycerol / Q000737:chemistry; D006736:Horses; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical; D015233:Models, Statistical; D008962:Models, Theoretical; D009211:Myoglobin / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D013696:Temperature; D013997:Time Factors
D008024:Ligands; D009211:Myoglobin; D002248:Carbon Monoxide; D005990:Glycerol