Preferred conformation of the terminally blocked (Aib)10 homo‐oligopeptide: A long, regular 310‐helix
Preferred conformation of the terminally blocked (Aib)10 homo‐oligopeptide: A long, regular 310‐helix
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末端封闭 (Aib)10 同源寡肽的首选构象：长而规则的 310 螺旋
DOI：
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发表时间：
1991
期刊：
影响因子：
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通讯作者：
A. Santini
中科院分区：
文献类型：
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作者：
C. Toniolo;M. Crisma;G. Bonora;E. Benedetti;Benedetto Dl Blasio;V. Pavone;C. Pedone;A. Santini
通过5（4 H）-恶唑酮方法合成的十肽pBrBz-（Aib）10-OtBu在单斜晶系空间群C2/c中结晶，其中a = 43.901（2），B = 9.289（2），c = 34.746（3）A; β = 114.69（3）°; Z = 8。晶体含有与每个肽相关的一个水分子。用Patterson方法求解了结构，并对6819个观察到的反射进行了修正，R值为0.073。该肽采用规则的310螺旋结构，由8个N <$H.<$O <$C分子内1 ← 4（或C10）H键稳定。这项研究使我们能够非常详细地表征这种重要的肽二级结构。结晶态构象与基于溶液中的IR吸收和1H-NMR研究提出的建议一致。
The decapeptide pBrBz‐ (Aib)10‐OtBu, synthesized by the 5(4H)‐oxazolone method, crystallizes in the monoclinic space group C2/c with a = 43.901(2), b = 9.289(2), and c = 34.746(3) A; β = 114.69(3)°; and Z = 8. The crystals contain one molecule of water associated with each peptide. The structure has been solved by the Patterson method and refined to an R value of 0.073 for 6819 observed reflections. The peptide adopts a regular 310‐helical structure stabilized by eight NH …︁ OC intramolecular 1 ← 4 (or C10) H bonds. This study has allowed us to characterize this important peptide secondary structure in great detail. The crystal‐state conformation agrees well with proposals made on the basis of an ir absorption and 1H‐nmr study in solution.
影响因子：
56.9
作者：
SUNDARALINGAM, M;SEKHARUDU, YC
通讯作者：
SEKHARUDU, YC