Premium
Solution conformation of endothelin, a potent vaso‐constricting bicyclic peptide A combined use 1 H NMR spectroscopy and distance geometry calculations
Author(s) -
Sharon L. A. Munro,
David J. Craik,
Christopher F McConville,
Jon G. Hall,
Mark S. Searle,
Wendy Bicknell,
Denis B. Scanlon,
Clive Chandler
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80071-a
Subject(s) - chemistry , conformational isomerism , peptide , bicyclic molecule , nuclear magnetic resonance spectroscopy , stereochemistry , crystallography , spectroscopy , molecule , physics , biochemistry , organic chemistry , quantum mechanics
The solution structure of endothelin 1, a newly discovered potent bicyclic peptide vaso‐constrictor agent, has been investigated using 1 H NMR conformational constraints and distance geometry calculations. The conformation is constrained by two disulphide bridges between Cys 1 ‐Cys 11 and Cys 1 Cys 11 but the NMR data and computed conformers show additional helical structure between residues Leu 4 and Cys 11 . Our results are compared with previous conflicting reports on the solution conformation on this peptide.