13C nuclear magnetic resonance studies of the conformation of the X-Pro bond in the oligopeptide hormones, thyrotropin-releasing hormone, luteinizing hormone-releasing factor, angiotensin and melanocyte-stimulating hormone release-inhibiting factor
- 2 July 1973
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 53 (1), 244-250
- https://doi.org/10.1016/0006-291x(73)91426-5
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Carbon-13 Chemical Shifts Accompanying Helix FormationCanadian Journal of Biochemistry, 1973
- Carbon-13 and Proton Nuclear Magnetic Resonance Observations of the Conformation of Poly(L-proline) in Aqueous Salt SolutionsMacromolecules, 1973
- Manifestation in the 13C‐NMR spectra of two different molecular conformations of a cyclic pentapeptideFEBS Letters, 1972
- A carbon-13 nuclear magnetic resonance study of oxytocin and its oligopeptidesBiochemical and Biophysical Research Communications, 1972
- Investigation of the Structure of Angiotensin II Using 13C Nuclear‐Magnetic‐Resonance SpectraEuropean Journal of Biochemistry, 1972
- Nuclear magnetic resonance spectroscopy. Carbon-13 chemical shifts of small peptides as a function of pHJournal of the American Chemical Society, 1972
- Helix-coil transition of a synthetic polypeptide monitored by Fourier transform carbon-13 nuclear magnetic resonanceJournal of the American Chemical Society, 1972
- 13C nuclear magnetic resonance spectroscopy and cis/trans isomerism in dipeptides containing prolineJournal of the Chemical Society, Chemical Communications, 1972
- Gonadotropin-Releasing Hormone: One Polypeptide Regulates Secretion of Luteinizing and Follicle-Stimulating HormonesScience, 1971
- Structure of porcine thyrotropin-releasing hormoneBiochemistry, 1970