Assignment of heme and distal amino acid resonances in the 1H-NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin
- 1 November 1985
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 832 (2) , 175-185
- https://doi.org/10.1016/0167-4838(85)90329-2
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Reaction of myoglobin with phenylhydrazine: a molecular doorstopBiochemistry, 1984
- Real space refinement of neutron diffraction data from sperm whale carbonmonoxymyoglobinJournal of Molecular Biology, 1981
- Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobinNature, 1981
- Solvent viscosity and protein dynamicsBiochemistry, 1980
- Structure and refinement of oxymyoglobin at 1·6 Å resolutionJournal of Molecular Biology, 1980
- Dynamics of ligand binding to heme proteinsJournal of Molecular Biology, 1979
- Temperature-dependent X-ray diffraction as a probe of protein structural dynamicsNature, 1979
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977
- Structural studies of hemes and hemoproteins by nuclear magnetic resonance spectroscopyPublished by Springer Nature ,1970