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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Betawrap: Successful prediction of parallel β-helices from primary sequence reveals an association with many microbial pathogens
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Betawrap: Successful prediction of parallel β-helices from primary sequence reveals an association with many microbial pathogens

机译:Betawrap:从一级序列成功预测平行β-螺旋揭示了与许多微生物病原体的关联

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摘要

The amino acid sequence rules that specify β-sheet structure in proteins remain obscure. A subclass of β-sheet proteins, parallel β-helices, represent a processive folding of the chain into an elongated topologically simpler fold than globular β-s heets. In this paper, we present a computational approach that predicts the right-handed parallel βhelix supersecondary structural motif in primary amino acid sequences by using β-strand interactions learned from non-β-helix structures. A program call ed BETAWRAP (Http.//theory.lcs.mit/betawrap)) implements this method and recognizes each of the seven known parallel β-helix families, when trained on the known parallel β-helices from outside that family.
机译:在蛋白质中指定β-折叠结构的氨基酸序列规则仍然不清楚。 β-折叠蛋白的一个亚类,平行的β-螺旋,代表链的逐步折叠,形成比球形β-sheets更长的拓扑简单折叠。在本文中,我们提出了一种计算方法,该方法通过使用从非β螺旋结构中获悉的β链相互作用来预测一级氨基酸序列中右手平行的β螺旋超二级结构基序。名为BETAWRAP(Http.//theory.lcs.mit/betawrap)的程序实现了此方法,并在该族以外的已知平行β螺旋上进行训练时,可以识别七个已知的平行β螺旋家族中的每一个。

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