Saudek V, Hoflack J, Pelton J T
Merrell Dow Research Institute, Strasbourg, France.
FEBS Lett. 1989 Oct 23;257(1):145-8. doi: 10.1016/0014-5793(89)81807-1.
The solution conformation of the recently discovered bi-cyclic, 21 amino acid vasoconstrictor peptide, Endothelin I, has been examined by 1H-NMR in deuterated dimethyl sulphoxide. A full sequential assignment has been achieved. In addition, 19 long range NOEs were detected which were employed as distance constraints in molecular dynamics calculations to yield a possible solution structure for this new peptide.
最近发现的双环21氨基酸血管收缩肽内皮素I的溶液构象，已在氘代二甲基亚砜中通过1H-NMR进行了研究。已完成了完整的序列归属。此外，还检测到19个长程核Overhauser效应（NOE），这些效应在分子动力学计算中用作距离约束，以产生这种新肽的一种可能的溶液结构。
