Nuclear magnetic resonance titration curves of histidine ring protons. The effect of temperature on ribonuclease A.
Open Access
- 1 September 1975
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 250 (18) , 7456-7460
- https://doi.org/10.1016/s0021-9258(19)40966-6
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Reassignment of the active site histidines in ribonuclease A by selective deuteration studiesBiopolymers, 1975
- Observation of histidine residues in proteins by nuclear magnetic resonance spectroscopyAccounts of Chemical Research, 1975
- The structure of ribonuclease at 2.5 Ångström resolutionJournal of Molecular Biology, 1974
- PROTON FOURIER TRANSFORM NMR STUDIES OF THE UNFOLDING OF RIBONUCLEASEAnnals of the New York Academy of Sciences, 1973
- Assignment of an exchangeable low-field nitrogen-hydrogen proton resonance of ribonuclease A to the active-site hisitidine-119Biochemistry, 1973
- Nuclear magnetic resonance titration curves of histidine ring protonsJournal of Molecular Biology, 1972
- Calorimetric study of thermally induced conformational transitions of ribonuclease A and certain of its derivativesBiochemistry, 1970
- Proton Magnetic Resonance Studies of Human LysozymeNature, 1969
- Nuclear magnetic resonance studies of the structure and binding sites of enzymes. VII. Solvent and temperature effects on the ionization of histidine residues of ribonucleaseBiochemistry, 1969
- Structural Studies of Ribonuclease. VI. Abnormal Ionizable Groups1-3Journal of the American Chemical Society, 1961