pH-dependence of 13C chemical shifts and 13C,H coupling constants in imidazole and L-histidine.
- 1 June 1975
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 147 (3), 605-607
- https://doi.org/10.1042/bj1470605
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Carbon-13 nuclear magnetic resonance studies of structure and function in thyrotropin-releasing factor. Determination of the tautomeric form of histidine and relation to biology activityBiochemistry, 1974
- Carbon-13 nuclear magnetic resonance studies of 85% carbon-13 enriched amino acids. Chemical shifts, coupling constants JC-C, and conformationJournal of the American Chemical Society, 1974
- Carbon-13 nuclear magnetic resonance titration shifts in amino acidsJournal of the American Chemical Society, 1974
- Carbon nuclear magnetic resonance studies of the histidine residue in α-lytic protease. Implications for the catalytic mechanism of serine proteasesBiochemistry, 1973
- Nuclear magnetic resonance titration curves of histidine ring protons. IV. The effects of phosphate and sulfate on ribonuclease.1973
- Studies of macromolecular structure by carbon-13 nuclear magnetic resonance. II. Specific labeling approach to the study of histidine residues in proteinsJournal of the American Chemical Society, 1973
- Determination of the tautomeric form of the imidazole ring of L-histidine in basic solution by carbon-13 magnetic resonance spectroscopyJournal of the American Chemical Society, 1973
- Carbon‐13 Nuclear‐Magnetic‐Resonance Studies on Selected Amino Acids, Peptides, and ProteinsEuropean Journal of Biochemistry, 1973
- Nuclear magnetic resonance spectroscopy. Carbon-13 chemical shifts of small peptides as a function of pHJournal of the American Chemical Society, 1972
- Carbon-13 magnetic resonance studies of amino acids and peptidesJournal of the American Chemical Society, 1968