多肽IS4溶液构象的进一步NMR研究

Further NMR Investigation and Conformation\= Study of Polypeptide IS4

利用二维核磁共振技术对多肽ＩＳ４中除Ｓｅｒ－１外的所有残基质子进行了指认．积分ＮＯＥＳＹ谱中的相关峰可得到距离约束．二面角的约束来自偶合常数３ＪＮＨα．由慢交换质子可得到氢键的约束．在进行距离几何程序计算时利用这些约束可得到一组构象，用能量最优化程序优化后的结果表明。

Two\|dimensional \{\}\+1H NMR technique was used to determine the solution structure of IS4. The cross\|peaks volumes in NOESY spectra were used to generate proton\|proton distance constraints. These data, combined with hydrogen bond constraints and angle constraints, were used to obtain a set of 10 structures by program DIANA. These structures were refined by unrestrained energy minimization using standard minimization program. The results indicated that the conformation of IS4 in CF\-3CD\-2OD is of \|helix.