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首页> 外文期刊>Journal of Molecular Biology >Analysis and Design of Turns in alpha-Helical Hairpins.
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Analysis and Design of Turns in alpha-Helical Hairpins.

机译：α-螺旋发夹的转弯分析和设计。

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Although the analysis and design of turns that connect the strands in antiparallel beta-hairpins has reached an advanced state, much less is known concerning turns between antiparallel helices in helical hairpins. We have conducted an analysis of the structures and sequence preferences of two types of interhelical turns, each of which connects the two helices by a two-residue linker in an alpha(L)-beta conformation. Based on this analysis, it became apparent that the turn introduced into a designed four-helix bundle protein, DF1, did not occur within an optimal structural context. DF1 is a dimeric model for the diiron class of proteins. A longer loop with a beta-alpha(R)-beta conformation was inserted between two helices in the protein, and a sequence was chosen to stabilize its conformation. X-ray crystallography and NMR analysis of the protein showed the structure to be in excellent agreement with design.
机译：尽管将反平行β-发夹中的链连接起来的转弯的分析和设计已达到高级状态，但对于螺旋发夹中的反平行螺旋之间的转弯，知之甚少。我们已经对两种类型的螺旋间转体的结构和序列偏好进行了分析，每种螺旋间转体通过两个残基的连接体以alpha（L）-β构型连接两个螺旋。基于此分析，很明显，导入最佳设计的四链螺旋蛋白DF1的转角不会发生。 DF1是蛋白质的二价铁二元模型。将具有β-alpha（R）-β构象的较长环插入蛋白质的两个螺旋之间，并选择一个序列来稳定其构象。蛋白质的X射线晶体学和NMR分析表明该结构与设计非常吻合。

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