Nuclear magnetic resonance studies of hemoproteins IV. Hindered rotation of heme side methyl group as a probe for studying van der waals contacts in the heme side environments of myoglobin derivatives
- 29 April 1975
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 386 (2) , 542-555
- https://doi.org/10.1016/0005-2795(75)90298-6
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- 220 MHz proton NMR studies of hemoproteins High-spin-low-spin equilibrium in ferric myoglobin and hemoglobin derivativesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1974
- Nuclear magnetic resonance studies of hemoproteins. III. Restricted rotation of a heme side chain methyl group in some ferric myoglobin complexes and its implication in van der Waals contact in the heme side chain environmentsJournal of the American Chemical Society, 1974
- Nuclear magnetic resonance studies of hemoproteins. Unusual temperature dependence of hyperfine shifts and spin equilibrium in ferric myoglobin and hemoglobin derivativesJournal of the American Chemical Society, 1974
- Assignments of the paramagnetically shifted heme methyl nuclear magnetic resonance peaks of cyanometmyoglobin by selective deuterationJournal of Molecular Biology, 1974
- Restricted rotation involving the tetrahedral carbon. V. Direct observation of the hindered rotation of a methyl group by high resolution nuclear magnetic resonance spectroscopyJournal of the American Chemical Society, 1973
- Proton nuclear magnetic resonance and electron spin resonance investigation of the electronic structure and magnetic properties of synthetic low-spin ferric porphyrinsJournal of the American Chemical Society, 1973
- Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of AllosteryNature, 1970
- Structural studies of hemes and hemoproteins by nuclear magnetic resonance spectroscopyPublished by Springer Nature ,1970
- Analysis of thermal equilibrium between high-spin and low-spin states in ferrihemoglobin complexesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1969
- Analysis of thermal equilibrium between high-spin and low-spin states in ferrimyoglobin complexesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1969