PROTEIN TERTIARY STRUCTURE RECOGNITION USING OPTIMIZED HAMILTONIANS WITH LOCAL INTERACTIONS
PROTEIN TERTIARY STRUCTURE RECOGNITION USING OPTIMIZED HAMILTONIANS WITH LOCAL INTERACTIONS
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DOI：
10.1073/pnas.89.19.9029
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发表时间：
1992-10-01
影响因子：
11.1
通讯作者：
WOLYNES, PG
中科院分区：
文献类型：
--
作者：
GOLDSTEIN, RA;LUTHEYSCHULTEN, ZA;WOLYNES, PG
蛋白质折叠代码体现本地的相互作用，包括表面和二级结构的倾向和残基残基的接触进行了优化，通过使用自旋玻璃理论的一组训练蛋白质。基于这些代码的筛选方法以100%的准确度将一组测试蛋白质的结构与具有相似拓扑结构的蛋白质正确匹配，即使测试蛋白质与结构同源物之间的序列相似性有限并且训练集中不存在任何结构相似的蛋白质。
Protein folding codes embodying local interactions including surface and secondary structure propensities and residue-residue contacts are optimized for a set of training proteins by using spin-glass theory. A screening method based on these codes correctly matches the structure of a set of test proteins with proteins of similar topology with 100% accuracy, even with limited sequence similarity between the test proteins and the structural homologs and the absence of any structurally similar proteins in the training set.