Nuclear magnetic resonance titration curves of histidine ring protons. Ribonuclease S-peptide and S-proteins.
Open Access
- 1 May 1976
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 251 (9) , 2648-2652
- https://doi.org/10.1016/s0021-9258(17)33537-8
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Observation of histidine residues in proteins by nuclear magnetic resonance spectroscopyAccounts of Chemical Research, 1975
- Nuclear magnetic resonance studies of the unfolding of pancreatic ribonuclease: I. Thermal and acid unfoldingJournal of Molecular Biology, 1975
- Experimental and Theoretical Aspects of Protein FoldingAdvances in Protein Chemistry, 1975
- A hypothesis for the pathway of the thermally-induced unfolding of bovine pancreatic ribonucleaseJournal of Theoretical Biology, 1975
- The structure of ribonuclease at 2.5 Ångström resolutionJournal of Molecular Biology, 1974
- Interaction of S-protein with S-peptide and with synthetic S-peptide analogs. Spectroscopic and calorimetric investigationBiochemistry, 1972
- Helix-coil transition of the isolated amino terminus of ribonucleaseBiochemistry, 1971
- Calorimetric study of thermally induced conformational transitions of ribonuclease A and certain of its derivativesBiochemistry, 1970
- Assignment of the histidine peaks in the nuclear magnetic resonance spectrum of ribonuclease.Proceedings of the National Academy of Sciences, 1968
- [76a] Preparation of ribonuclease S and its component parts, S-peptide and S-proteinPublished by Elsevier ,1967