Chou K C
Pharmacia & Upjohn, Kalamazoo, Michigan, USA.
J Pept Res. 1997 Feb;49(2):120-44.
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.
提出了一种残基耦合模型来预测蛋白质中的β-转角。训练数据库中455个β-转角四肽和3807个非β-转角四肽的正确预测率分别为94.7%和81.3%。测试数据库中110个β-转角四肽和30229个非β-转角四肽的正确预测率分别为80.0%和80.2%。与之前报道的基于残基独立模型的正确预测率相比,新模型显著提高了预测质量,这意味着在蛋白质折叠过程中,多肽链上的残基耦合效应对于诸如β-转角等反向转角的形成很重要。