Conformational analysis of linear peptides by 15N NMR spectroscopy using the enkephalin‐related fragmetn Tyr—Gly—Gly—Phe as a model compound
- 30 June 1980
- journal article
- Published by Wiley in FEBS Letters
- Vol. 115 (2) , 315-318
- https://doi.org/10.1016/0014-5793(80)81196-3
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Conformational analysis by nuclear magnetic resonance spectroscopy: Nitrogen-15 NMR of a cyclic pentapeptideJournal of the American Chemical Society, 1979
- A study of the peptide hormone oxytocin and of prolylleucylglycinamide by nitrogen-15 NMRJournal of the American Chemical Society, 1979
- Hydrogen-deuterium substitution and solvent effects on the nitrogen-15 nuclear magnetic resonance of gramicidin S: evaluation of secondary structureBiochemistry, 1978
- A nitrogen-15 spin-lattice relaxation study of alumichromeBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Enkephalin related fragments, conformational studies of the tetrapeptides Tyr-Gly-Gly-Phe and Gly-Gly-Phe-X (X = Leu, met) by X-ray and 1H NMR spectroscopyBiochemical and Biophysical Research Communications, 1977
- Proton magnetic resonance studies of conformation and flexibility of enkephalin peptidesNature, 1976
- Conformation of Met5-enkephalin determined by high field PMR spectroscopyNature, 1976
- Natural abundance nitrogen-15 nuclear magnetic resonance spectroscopy. Medium effects on the nitrogen-15 chemical shifts of small peptidesJournal of the Chemical Society, Perkin Transactions 2, 1976
- pH Dependence of the 15N and 17O nuclear magnetic resonance chemical shifts of glycylglycineJournal of the Chemical Society, Chemical Communications, 1976
- Theory and practice for studies of peptides by 15N nuclear magnetic resonance at natural abundance: gramicidin SNature, 1975