Article
1H NMR investigation of distal mutant deoxy myoglobins. Interpretation of proximal His contact shifts in terms of a localized distal water molecule.
The Journal of biological chemistry - 25 Nov 1994
La Mar G N, Dalichow F, Zhao X, Dou Y, Ikeda-Saito M, Chiu M L, Sligar S G
Abstract excerpt
1H NMR spectra of a series of distal point mutants of human and sperm whale deoxy myoglobin have been recorded and their spectral parameters compared with those of wild type. The substitutions investigated include His64(E7)-->Gly, Ala, Val, Leu, Ile, and Gln and Val68(E11)-->Ala, Ile. The three r...
Topics
- Animals
- Histidine
- Humans
- Magnetic Resonance Spectroscopy
- Mutation
- Myoglobin
- Protons
- Water
- Whales
