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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >A complete Fourier-synthesis-based backbone- conformation-dependent library for proteins
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A complete Fourier-synthesis-based backbone- conformation-dependent library for proteins

机译：一个完整Fourier-synthesis-based骨干-conformation-dependent库蛋白质

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摘要

While broadening the applicability of (φ/Ψ) -dependent target values for the bond angles in the peptide backbone, sequence/conformation categories with too few residues to analyze via previous methods were encountered. Here, a method of describing a conformation-dependent library (CDL) using two-dimensional Fourier coefficients is reported where the number of coefficients for individual categories is determined via complete cross-validation. Sample sizes are increased further by selective blending of categories with similar patterns of conformational dependence. An additional advantage of the Fourier-synthesis-based CDL is that it uses continuous functions and has no artifactual steps near the edges of populated regions of φ/Ψ space. A set of libraries for the seven main-chain bond angles, along with the ω and ζ, angles, was created based on a set of Fourier analyses of 48 368 residues selected from high-resolution models in the wwPDB. This new library encompasses both trans- and cis-peptide bonds and outperforms currently used discrete CDLs.
机译：而扩大的适用性(φ/Ψ)端依赖目标键角的值肽链序列/构象类别与残留分析太少以前的方法。描述一个conformation-dependent库(CDL)使用二维傅里叶系数据报道系数的数量在哪里通过完成单个类别确定交叉验证。进一步通过选择性混合的类别类似的构象依赖模式。额外的优势Fourier-synthesis-based CDL是它的用途连续函数和没有artifactual步骤填充区域的边缘附近的φ/Ψ空间。图书馆的一组七个主链键角,ω和ζ,角,创建基于一组48的傅里叶分析368年残留物从高分辨率的选择模型wwPDB。反式- - -顺式债券和优于目前使用离散的情况。

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