1H NMR titration shifts of amide proton resonances in polypeptide chains
- 1 May 1977
- journal article
- Published by Wiley in FEBS Letters
- Vol. 77 (1) , 11-14
- https://doi.org/10.1016/0014-5793(77)80182-8
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- Nmr studies of aqueous solutions of tetra and branched peptides. I. Sequence determination of amino‐acid residues and the assignment of peptide hydrogen signalsBiopolymers, 1976
- Studies of peptide conformation: Backbone folding of tetrapeptide derivatives in methanol and waterBiopolymers, 1976
- Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI)European Biophysics Journal, 1976
- Solution conformation of the ferrichromes. VI. Charge relay at the peptide bond. Proton magnetic resonance study of solvation effects on the amide electron density distributionJournal of the American Chemical Society, 1975
- Carbon-13 NNIR of the protected tetrapeptides TFA-Gly-Gly-L-X-L-Ala-OCH3, where X stands for the 20 common amino acidsJournal of Magnetic Resonance (1969), 1974
- Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitorFEBS Letters, 1973
- Nuclear magnetic resonance study of bovine pancreatic trypsin inhibitor. Tyrosine titrations and backbone NH groupsBiochemistry, 1973
- The γ Turn, a Possible Folded Conformation of the Polypeptide Chain. Comparison with the β TurnMacromolecules, 1972
- Temperature dependence of amide proton chemical shifts: The secondary structures of gramicidin S and valinomycinBiochemical and Biophysical Research Communications, 1969