Coupling of protein relaxation to ligand binding and migration in myoglobin

Noam Agmon*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

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 languageEnglish
Pages (from-to)1537-1543
Number of pages7
JournalBiophysical Journal
Volume87
Issue number3
DOIs
StatePublished - Sep 2004

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