1H NMR investigation of distal mutant deoxy myoglobins. Interpretation of proximal His contact shifts in terms of a localized distal water molecule.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference50 articles.
1. NMR Spectroscopy of Paramagnetic Haem Proteins
2. Determination of the orientation of the magnetic axes of the cyano-MetMb complexes of point mutants of myoglobin by solution 1H NMR: influence of his E7 .fwdarw. Gly and Arg CD3 .fwdarw. Gly substitutions
3. Solution structure determination of the heme cavity in the E7 His .fwdarw. Val cyano-Met myoglobin point mutant based on the proton NMR detected dipolar field of the iron: Evidence for contraction of the heme pocket
4. Proton NMR hyperfine shift pattern as a probe for ligation state in high-spin ferric hemoproteins: water binding in metmyoglobin mutants
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