Article
Structural and functional effects of apolar mutations of the distal valine in myoglobin.
Journal of molecular biology - 27 Jan 1995
Quillin M L, Li T, Olson J S, Phillips G N, Dou Y, Ikeda-Saito M, Regan R, Carlson M, Gibson Q H, Li H
Abstract excerpt
High-resolution structures of the aquomet, deoxy, and CO forms of Ala68, Ile68, Leu68, and Phe68 sperm whale myoglobins have been determined by X-ray crystallography. These 12 new structures, plus those of wild-type myoglobin, have been used to interpret the effects of mutations at position 68 and the effects of cobalt substitution on the kinetics of O2, CO, and NO binding. Molecular dynamics simulations based on...
Topics
- Animals
- Carbon Monoxide
- Kinetics
- Ligands
- Mutation
- Myoglobin
- Nitric Oxide
- Oxygen
- Protein Binding
- Valine
- Water
- Whales