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采用苯甲酰甲酯作为α-羧基的暂时性保护基,以片段缩合的方式合成了疏水性多肽-鼠脑钠通道I的IS3片段,利用高效液相色谱对其进行了纯化,并通过了氨基酸组成分析和朱子轰击质谱鉴定。 相似文献
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多肽IS4溶液构象的进一步NMR研究 总被引:1,自引:1,他引:0
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,多肽IS4在CF3CD2OH中的构象为α-螺旋. 相似文献
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We used CD spectroscopy to study the conformations of three cyclic peptides (CP10E: cyclo[Glu(OBz1)-Pro-Gly-Glu(OBzl)-Gly]2, CP10K: cyclo[Lys(Z)-Pro-Gly-Lys(Z)-Gly]2, CP12K: cyclo[Phe-Lys(Z)-Pro-Gly-Lys(Z)-Gly]2 and their correspondent linear peptides (LP10E: Boc-[Glu(OBzl)-Pro-Gly-Glu(OBzl)-Gly]2-OPac, LP10K: Boc-[Lys(Z)-Pro-Lys(Z)-Pro]2-OMe, LP 12K: Bao- [-Lys(Z)-Pro-Gly-Lys(Z)-Gly]2- OMe) in three solvents of different polarity (chloroform, acetonitrile, 2,2,2-triliuroethanol), and it was found that all of linear and cyclicpeptides exists asγ-turn conformation in chloroform, however, in TFE& CH3CN solutions, the three linear peptides are inβ Ⅱ-turn conformations. CP10E isβI-turn conformation, CP10K &CP12K exists in more than one types of turn conformations. On the basis of our experiments, it was concluded: 1) In the presence of conformational constrained amino acids short linear peptides form obvious secondary structure; 2)The solvent polarity has influence on the peptide conformation and this influence on linear peptides is greater than that on cyclic peptides; 3)The backbone of cyclic peptide has constraint effect on its conformation and makes the secondary structure of cyclic peptide different from that of its relative linear peptide. This information might give some cules in the design of bioactive peptides with different receptor selectivity. 相似文献
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采用本甲酸甲酯作为α-羧基的暂时性保护基,以片段缩合的方式合成了疏水性多肽──鼠脑钢通道Ⅰ的IS3片段,利用高效液相色谱对其进行了纯化,并通过了氨基酸组成分析和快原子轰击质谱鉴定. 相似文献
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