Solution conformation of endothelin determined by nuclear magnetic resonance and distance geometry.
作者： Satoshi Endo , Hiroshi Inooka , Yoshihiro Ishibashi , Chieko Kitada , Eiji Mizuta
DOI: 10.1016/0014-5793(89)81808-3
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摘要: Abstract The solution conformation of endothelium-derived vasoconstrictor peptide, endothelin, has been determined by two-dimensional 1 H-NMR spectroscopy and distance geometry. Conformation in the N-terminal core region (residues 1–15) is well-defined a characteristic helix-like segment from Lys 9 to Cys 15 . Contrarily, C-terminal tail 16–21) does not assume defined there are no specific interactions between regions. Endothelin; Vasoconstrictor peptide; Three-dimensional structure; NMR, H; Distance geometry
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