Carbon-13 nuclear magnetic resonance study of the motional behavior of ethyl isocyanide bound to myoglobin and hemoglobin
- 1 May 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (11) , 2273-2279
- https://doi.org/10.1021/bi00578a022
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Assignment of the carbon-13 nuclear magnetic resonance spectrum of aqueous ganglioside GM1 micellesBiochemistry, 1978
- Nuclear magnetic resonance studies on bacterial dihydrofolate reductase containing [methyl-13C]methionineBiochemistry, 1978
- Kinetics of hemoglobin and transition state theory.Proceedings of the National Academy of Sciences, 1978
- Quantitative determination of carbamino adducts of alpha and beta chains in human adult hemoglobin in presence and absence of carbon monoxide and 2,3-diphosphoglycerate.Journal of Biological Chemistry, 1977
- Studies of proteins in solution by natural-abundance carbon-13 nuclear magnetic resonance. Spectral resolution and relaxation behavior at high magnetic field strengthsJournal of the American Chemical Society, 1977
- Determination of rotational correlation times of proteins in solution from carbon-13 spin-lattice relaxation measurements. Effect of magnetic field strength and anisotropic rotationJournal of the American Chemical Society, 1976
- Nuclear magnetic resonance studies of sperm whale myoglobin specifically enriched with 13C in the methionine methyl groups.Journal of Biological Chemistry, 1976
- The effect of ligand size and stereochemistry on the reactivity of the α and β chains within hemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- Carbon-13 NMR studies of C2H5N13C binding to various hemoproteinsBiochemical and Biophysical Research Communications, 1976
- COMPARISON OF MYOGLOBINS FROM HARBOR SEAL PORPOISE AND SPERM WHALE .I. PREPARATION AND CHARACTERIZATION1968