Solution conformation of endothelin determined by nuclear magnetic resonance and distance geometry |
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Authors: | S Endo H Inooka Y Ishibashi C Kitada E Mizuta M Fujino |
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Affiliation: | Tsukuba Research Laboratories, Takeda Chemical Industries Ltd, Japan. |
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Abstract: | The 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. |
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