Determining dihedral angles and local structure in silk peptide by 13C-2H REDOR
Determining dihedral angles and local structure in silk peptide by 13C-2H REDOR
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DOI：
10.1021/ja0342345
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发表时间：
2003-06-25
影响因子：
15
通讯作者：
Asakura, T
中科院分区：
文献类型：
--
作者：
Gullion, T;Kishore, R;Asakura, T
对30个残基（AlaGly）的15丝素I模拟物进行13 C − 2 H REDOR NMR实验，以获得关于丝素I构象的难以捉摸的结构的结构细节。13 C，2 H-标记策略被说明用于测量肽中的单个二面角和用于通过REDOR确定局部结构。在Gly（14）-Ala（17）区域发现了II型性状的主要转折。
13C−2H REDOR NMR experiments were performed on 30-residue (AlaGly)15silk I mimics ofBombyx morisilk fibroin to gain structural details about the elusive structure of the silk I conformation.13C,2H-labeling strategies are illustrated for measuring individual dihedral angles in peptides and for determining local structure by REDOR. A major turn of type II character is found in the region Gly(14)-Ala(17).