SECONDARY STRUCTURAL PREDICTION OF PROTEINS FROM THEIR AMINO-ACID SEQUENCE
SECONDARY STRUCTURAL PREDICTION OF PROTEINS FROM THEIR AMINO-ACID SEQUENCE
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DOI：
10.1016/0968-0004(77)90440-6
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发表时间：
1977-01-01
影响因子：
13.8
通讯作者：
FASMAN, GD
中科院分区：
文献类型：
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作者：
CHOU, PY;FASMAN, GD
为了充分理解蛋白质生物活性的基本原理，有必要了解它们的空间构象。X射线衍射技术已经成功地阐明了60多种蛋白质的三维结构(构象)[1，2]。由于这类研究费用昂贵，费时费力，而且需要合适的晶体，因此已经探索了其他方法来提供结构信息。由于蛋白质的天然构象是在其氨基酸序列中编码的[3]，人们已经做出了许多努力来从序列数据中预测蛋白质的结构。早期研究(回顾见4)尝试使用物理化学数据(光学旋转色散等)。将氨基酸组成和蛋白质的螺旋含量联系起来。随着X射线数据的获得，基于已知的氨基酸序列和由晶体研究描绘的二级结构的各种预测方案被开发出来[4]。由于篇幅有限，目前可用的各种预测算法[4]将不再详述，而是将简要描述周和法斯曼的方法[5，6]，并将其作为该方法的一个例子来展示其实用性。对已确定其X-射线结构的15个蛋白质进行了统计分析，并按其等级顺序建立了所有20个氨基酸的螺旋构象势和P-折叠构象势。关于这15种蛋白质中螺旋和/？片状边界残基的频率的广泛表格也发表了[S]。螺旋和B-折叠构象参数Pm
To fully comprehend the rationale of bio-logical activity of proteins, it is necessary to have a knowledge of their spatial conformation. X-ray diffraction techniques have successfully elucidated the three dimensional structure (conformation) of over 60 proteins [1, 2]. Since such studies are expensive, laborious and require suitable crystals, other approaches have been explored to give structural information. As the native conformation of a protein is coded in its amino acid sequence [3], many efforts have been made to predict protein structure from sequence data. Early studies (for review see 4) attempted to use physical-chemical data (optical rotatory dispersion, etc.) to correlate amino acid composition and the helical content of proteins. As X-ray data became available, various predictive schemes were developed [4] based on the known amino acid sequence and the secondary structures delineated by the crystallographic studies.The various predictive algorithms, available at present [4], will not be elaborated on due to lack of space, but rather the method of Chou and Fasman [5, 6] will be briefly described and its utility demonstrated as an example of this approach. A statistical survey of 15 proteins, whose X-ray structure had been determined, was made and the helix and P-sheet conformational potentials of all 20 amino acids were established in their hierarchial order. Extensive tables on the frequency of helical and/?-sheet boundary residues in these 15 proteins were also published [S]. The helix and B-sheet conformational parameters Pm