Solution conformation of endothelin determined by nuclear magnetic resonance and distance geometry

Abstract

AbstractThe solution conformation of endothelium-derived vasoconstrictor peptide, endothelin, has been determined by two-dimensional 1H-NMR spectroscopy and distance geometry. Conformation in the N-terminal core region (residues 1–15) is well-defined and a characteristic is the helix-like conformation in the segment from Lys9 to Cys15. Contrarily, the C-terminal tail region (residues 16–21) does not assume a defined conformation and there are no specific interactions between the core and the tail regions.Endothelin; Vasoconstrictor peptide; Three-dimensional structure; NMR, 1H; Distance geometr