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β-转角类型的分类与预测。

Classification and prediction of beta-turn types.

作者信息

Chou K C, Blinn J R

机构信息

Pharmacia & Upjohn, Kalamazoo, Michigan 49007-4940, USA.

出版信息

J Protein Chem. 1997 Aug;16(6):575-95. doi: 10.1023/a:1026366706677.

DOI:10.1023/a:1026366706677
PMID:9263121
Abstract

Although a beta-turn consists of only four amino acids, it assumes many different types in proteins. Is this basically dependent on the tetrapeptide sequence alone or is it due to a variety of interactions with the other part of a protein? To answer this question, a residue-coupled model is proposed that can reflect the sequence-coupling effect for a tetrapeptide in not only a beta-turn or non-beta-turn, but also different types of a beta-turn. The predicted results by the model for 6022 tetrapeptides indicate that the rates of correct prediction for beta-turn types I, I', II, II', VI, and VIII and non-beta-turns are 68.54%, 93.60%, 85.19%, 97.75%, 100%, 88.75%, and 61.02%, respectively. Each of these seven rates is significantly higher than 1/7 = 14.29%, the completely randomized rate, implying that the formation of different beta-turn types or non-beta-turns is considerably correlated with the sequences of a tetrapeptide.

摘要

尽管β-转角仅由四个氨基酸组成,但它在蛋白质中呈现出多种不同类型。这主要仅取决于四肽序列,还是由于与蛋白质其他部分的多种相互作用所致?为回答这个问题,提出了一种残基偶联模型,该模型不仅可以反映四肽在β-转角或非β-转角中,而且可以反映在不同类型β-转角中的序列偶联效应。该模型对6022个四肽的预测结果表明,对I型、I'型、II型、II'型、VI型和VIII型β-转角以及非β-转角的正确预测率分别为68.54%、93.60%、85.19%、97.75%、100%、88.75%和61.02%。这七个比率中的每一个都显著高于完全随机比率1/7 = 14.29%,这意味着不同类型的β-转角或非β-转角的形成与四肽序列密切相关。

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本文引用的文献

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J Pept Res. 1997 Feb;49(2):120-44.
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A revised set of potentials for beta-turn formation in proteins.一组经修订的蛋白质中β-转角形成的势能。
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Prediction of protein structural classes.蛋白质结构类别的预测。
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Improving Protein Gamma-Turn Prediction Using Inception Capsule Networks.利用 inception 胶囊网络提高蛋白质 γ-转角预测。
Sci Rep. 2018 Oct 24;8(1):15741. doi: 10.1038/s41598-018-34114-2.
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Identify Beta-Hairpin Motifs with Quadratic Discriminant Algorithm Based on the Chemical Shifts.基于化学位移,用二次判别算法识别β-发夹基序。
PLoS One. 2015 Sep 30;10(9):e0139280. doi: 10.1371/journal.pone.0139280. eCollection 2015.
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Insight into a molecular interaction force supporting peptide backbones and its implication to protein loops and folding.对支持肽主链的分子相互作用力及其对蛋白质环和折叠的影响的洞察。
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Coarse-grained, foldable, physical model of the polypeptide chain.多肽链的粗粒度、可折叠的物理模型。
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The anatomy and taxonomy of protein structure.蛋白质结构的解剖学与分类学。
Adv Protein Chem. 1981;34:167-339. doi: 10.1016/s0065-3233(08)60520-3.
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Biopolymers. 1983 Dec;22(12):2577-637. doi: 10.1002/bip.360221211.
6
Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units.多肽和蛋白质的立体化学标准。V. 三个相连肽单元系统的构象
Biopolymers. 1968 Oct;6(10):1425-36. doi: 10.1002/bip.1968.360061006.
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Structure of rubredoxin: an x-ray study to 2.5 A resolution.红氧还蛋白的结构:分辨率达2.5埃的X射线研究。
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Biochemistry. 1974 Jan 15;13(2):211-22. doi: 10.1021/bi00699a001.
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