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首页> 外文期刊>Journal of the American Chemical Society >First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two L-Val Residues. Crystal and Solution Structure of Boc-L-Val-ΔPhe-ΔPhe-ΔPhe-L-Val-OMe
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First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two L-Val Residues. Crystal and Solution Structure of Boc-L-Val-ΔPhe-ΔPhe-ΔPhe-L-Val-OMe

机译:首次观察到含有两个L-Val残基的脱氢肽中的左旋螺旋构象。 Boc-L-Val-ΔPhe-ΔPhe-ΔPhe-L-Val-OMe的晶体和溶液结构

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摘要

The solution and solid structure of Boc-L-Val-ΔPhe-ΔPhe-ΔPhe-L-Val-OMe, containing three consecutive ΔPhe residues, have been determined by X-ray diffraction, nuclear magnetic resonance, and circular dichroism methods. The crystals grown from aqueous methanol are orghorhombic, space group P2_12_12_1, a=aa.624(2), b=17.248(2), c=21.532 ?, V=4216(1) ?~3, Z=4. In the solid state, the peptide exhibits a left-handed 3_10-helical conformation, in spite of the presence of two L-Val residues.
机译:通过X射线衍射,核磁共振和圆二色性方法确定了Boc-L-Val-ΔPhe-ΔPhe-ΔPhe-L-Val-OMe的溶液和固体结构,该溶液包含三个连续的ΔPhe残基。从甲醇水溶液中生长的晶体是正交晶体,空间群为P2_12_12_1,a = aa.624(2),b = 17.248(2),c = 21.532532,V = 4216(1)~~ 3,Z = 4。在固态下,尽管存在两个L-Val残基,该肽仍显示出左旋3_10-螺旋构象。

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