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引用次数: 0

摘要

提出了一种残基耦合模型来预测蛋白质中的β -转变。训练数据库中455个β -turn四肽和3807个非β -turn四肽的预测正确率分别为94.7和81.3%。测试数据库中110个β -turn四肽和30229个非β -turn四肽的预测正确率分别为80.0和80.2%。与先前报道的基于残基无关模型的预测正确率相比,新模型的预测质量显著提高,这表明在蛋白质折叠过程中,沿多肽链的残基偶联效应对逆转旋的形成(如β旋)很重要。
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Prediction of beta-turns.

A residue-coupled model is proposed to predict the beta-turns in proteins. The rates of correct prediction for the 455 beta-turn tetrapeptides and 3807 non-beta-turn tetrapeptides in the training database are 94.7 and 81.3%, respectively. The rates of correct prediction for the 110 beta-turn tetrapeptides and 30,229 non-beta-turn tetrapeptides in the testing database are 80.0 and 80.2%, respectively. Compared with the rates of correct prediction based on the residue-independent model reported previously, the quality of prediction is significantly improved by the new model, implying that the residue-coupled effect along a polypeptide chain is important for the formation of reversal turns, such as beta-turns, during the process of protein folding.

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