Conformational heterogeneity in linear peptides in solution: A carbon‐13 NMR study of [Pro3, Pro5] ‐angiotensin‐II
- 1 February 1976
- journal article
- Published by Wiley in FEBS Letters
- Vol. 62 (1), 50-56
- https://doi.org/10.1016/0014-5793(76)80014-2
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Conformational flexibility of luteinizing hormone-releasing hormone in aqueous solution. Carbon-13 spin-lattice relaxation time studyBiochemistry, 1975
- High field carbon-13 NMR spectroscopy. Conformational mobility in gramicidin S and frequency dependence of 13C spin-lattice relaxation timesBiochemical and Biophysical Research Communications, 1975
- A 13C spin‐lattice relaxation study of dipeptides containing glycine and proline: Mobility of the cyclic proline side chainBiopolymers, 1975
- Conformational flexibility of angiotensin II. Carbon-13 spin-lattice relaxation studyBiochemistry, 1975
- Conformation of angiotensin II in aqueous solutions. Titration of several peptide analogs and homologsBiochemistry, 1974
- Conformation flexibility of the neurohypophyseal hormones oxytocin and lysine-vasopressin. Carbon-13 spin-lattice relaxation study of backbone and side chainsJournal of the American Chemical Society, 1974
- Study of internal rotations in gramicidin S by carbon-13 spin-lattice relaxation measurementsJournal of the American Chemical Society, 1973
- Carbon-13 magnetic resonance spectroscopy. Spectrum of proline in oligopeptidesThe Journal of Organic Chemistry, 1973
- 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