标题： 离散模型中具有良好折叠性质的氨基酸序列的识别 显示英文标题

标题： Identification of Amino Acid Sequences with Good Folding Properties in an Off-Lattice Model

摘要： 分析了一种仅包含疏水性和亲水性两种氨基酸类型的二维玩具蛋白质模型的折叠性质。 采用一种高效的蒙特卡罗方法，以确保找到基态。 与动力学性质不同，热力学性质被发现强烈依赖于序列。 因此，完全根据热力学涨落定义了良好的折叠标准。 利用这些标准，分离出了折叠效果好的序列模式。 对于由20个随机选择的二元残基组成的300条链，大约有10%符合这些标准。 此外，还通过统计学和人工神经网络方法进行了分析，得出结论：只要给定表征序列的二元数，就可以在一定程度上预测折叠性质。 显示英文摘要

摘要： Folding properties of a two-dimensional toy protein model containing only two amino-acid types, hydrophobic and hydrophilic, respectively, are analyzed. An efficient Monte Carlo procedure is employed to ensure that the ground states are found. The thermodynamic properties are found to be strongly sequence dependent in contrast to the kinetic ones. Hence, criteria for good folders are defined entirely in terms of thermodynamic fluctuations. With these criteria sequence patterns that fold well are isolated. For 300 chains with 20 randomly chosen binary residues approximately 10% meet these criteria. Also, an analysis is performed by means of statistical and artificial neural network methods from which it is concluded that the folding properties can be predicted to a certain degree given the binary numbers characterizing the sequences.