| Literature DB >> 15345534 |
Abstract
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.Mesh:
Substances:
Year: 2004 PMID: 15345534 PMCID: PMC1304560 DOI: 10.1529/biophysj.104.042929
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033