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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Structural class prediction: an application of residue distribution along the sequence
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Structural class prediction: an application of residue distribution along the sequence

机译：结构分类预测：残基沿序列分布的应用

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Deciphering the native conformation of proteins from their amino acid sequences is one of the most challenging problems in molecular biology. Information on the secondary structure of a protein can be helpful in understanding its native folded state. In our earlier work on molecular chaperones, we have analyzed the hydrophobic and charged patches, short-, medium- and long-range contacts and residue distributions along the sequence. In this article, we have made an attempt to predict the structural class of globular and chaperone proteins based on the information obtained from residue distributions. This method predicts the structural class with an accuracy of 93 and 96%, respectively, for the four- and three-state models in a training set of 120 globular proteins, and 90 and 96%, respectively, for a test set of 80 proteins. We have used this information and methodology to predict the structural classes of chaperones. Interestingly most of the chaperone proteins are predicted under alpha/beta or mixed folding type. (C) 2000 Elsevier Science B.V. All rights reserved. [References: 39]
机译：从其氨基酸序列解密蛋白质的天然构象是分子生物学中最具挑战性的问题之一。有关蛋白质二级结构的信息可能有助于理解其天然折叠状态。在我们早期的分子伴侣研究中，我们分析了疏水和带电荷的斑块，短，中和长距离接触以及沿序列的残基分布。在本文中，我们已尝试根据残基分布获得的信息预测球状蛋白和伴侣蛋白的结构类别。该方法在120个球状蛋白质训练集中的四态和三态模型中预测结构类别的准确度分别为93％和96％，在80种蛋白质的测试集中分别预测为90％和96％的准确度。我们已经使用此信息和方法来预测分子伴侣的结构类别。有趣的是，大多数伴侣蛋白被预测为α/β或混合折叠类型。 （C）2000 Elsevier Science B.V.保留所有权利。 [参考：39]

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