Heme orientational disorder in reconstituted and native sperm whale myoglobin
Authors:
- Gerd N. La MarGMGerd N. La Mar
- N.L. DavisNDN.L. Davis
- Daniel W. ParishDPDaniel W. Parish
- Kevin M. SmithKSKevin M. Smith
- 1 August 1983
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 168 (4) , 887-896
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Assignment of hyperfine-shifted resonances in low-spin forms of cytochrome c peroxidase by reconstitutions with deuterated heminsJournal of the American Chemical Society, 1983
- Proton nuclear magnetic resonance investigation of the nature of solution conformational equilibriums of monomeric insect deoxyhemoglobinsBiochemistry, 1981
- Structure and refinement of oxymyoglobin at 1·6 Å resolutionJournal of Molecular Biology, 1980
- Structure of erythrocruorin in different ligand states refined at 1·4 Å resolutionJournal of Molecular Biology, 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
- Assignments of the paramagnetically shifted heme methyl nuclear magnetic resonance peaks of cyanometmyoglobin by selective deuterationJournal of Molecular Biology, 1974
- Electronic structure of cyanide complexes of hemes and heme proteinsJournal of Molecular Biology, 1971
- Properties of Components of Myoglobin of the Sperm WhaleNature, 1964
- Cleavage of the haem-protein link by acid methylethylketoneBiochimica et Biophysica Acta, 1959