Proton magnetic resonance investigation of the influence of quaternary structure on the iron-histidine bonding in deoxyhemoglobins
- 2 March 1982
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 21 (5) , 842-847
- https://doi.org/10.1021/bi00534a005
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Haemoglobin: The structural changes related to ligand binding and its allosteric mechanismJournal of Molecular Biology, 1979
- Coupling between oxidation state and hydrogen bond conformation in heme proteinsProceedings of the National Academy of Sciences, 1979
- Absence of heme-localized strain in T state hemoglobin: insensitivity of heme-imidazole resonance Raman frequencies to quaternary structure.Proceedings of the National Academy of Sciences, 1979
- Extended X-ray absorption fine structure determination of iron nitrogen distances in haemoglobinNature, 1978
- Role of Bohr group salt bridges in cooperativity in hemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Self-association of hemoglobin β SH chains is linked to oxygenationProceedings of the National Academy of Sciences, 1978
- High-spin ferrous porphyrin complexes as models for deoxymyoglobin and -hemoglobin. A proton nuclear magnetic resonance studyJournal of the American Chemical Society, 1977
- Magnetic field and temperature induced line broadening in the hyperfine-shifted proton resonances of myoglobin and hemoglobinJournal of the American Chemical Society, 1977
- Structure-function relations in hemoglobin as determined by x-ray absorption spectroscopy.Proceedings of the National Academy of Sciences, 1976
- The properties and interactions of the isolated α and β chains of human haemoglobinJournal of Molecular Biology, 1965