首页> 外文期刊>Chemistry: A European journal >Unprecedented torsional preferences in trans-β ~(2,3)-amino acid residues and formation of 11-helices in α,β ~(2,3)-hybrid peptides
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Unprecedented torsional preferences in trans-β ~(2,3)-amino acid residues and formation of 11-helices in α,β ~(2,3)-hybrid peptides

机译:反式β〜(2,3)-氨基酸残基空前的扭转偏好以及α,β〜(2,3)-杂合肽中11螺旋的形成

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摘要

Anti or gauche? trans-β ~(2,3)-Amino acid residues that are known to promote extended structures in their peptides show specific rotamer preferences in response to an intramolecular hydrogen-bonding possibility, which facilitates the 11-helical structures in their 1:1 α,β-hybrid peptides (see figure). Preferences for the gauche conformation for all internal β residues and anti for the C-terminal residue in these peptides were confirmed by NMR spectroscopic and X-ray diffraction experiments.
机译:防还是薄纱?反-β〜(2,3)-已知可促进其肽中扩展结构的氨基酸残基在响应分子内氢键的可能性时表现出特定的rotamer偏好,从而促进其1:1α的11螺旋结构,β-杂合肽(见图)。通过NMR光谱和X射线衍射实验证实了这些肽中所有内部β残基的gauche构象的偏爱和C末端的抗gauche构象的偏爱。

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