ANALYSIS OF THE RELATIONSHIP BETWEEN SIDE-CHAIN CONFORMATION AND SECONDARY STRUCTURE IN GLOBULAR-PROTEINS
ANALYSIS OF THE RELATIONSHIP BETWEEN SIDE-CHAIN CONFORMATION AND SECONDARY STRUCTURE IN GLOBULAR-PROTEINS
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DOI：
10.1016/0022-2836(87)90314-7
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发表时间：
1987-11-20
影响因子：
5.6
通讯作者：
STERNBERG, MJE
中科院分区：
文献类型：
--
作者：
MCGREGOR, MJ;ISLAM, SA;STERNBERG, MJE
研究了优选的侧链二面角与残基的二级结构之间的关系。61种蛋白质的结构解析到2.0埃的分辨率。（1. = 0.1 nm）或更好的样品进行分析，使用关系数据库存储信息。观察到的最强特征是α-半乳糖苷酶中大多数侧链的χ 1分布当与非α/螺旋相比时，螺旋显示不存在G-构象，并向T构象移动。β的结构.这种趋势的例外是短极性侧链，它们与主链形成氢键，更喜欢g+。β-β-D中残基的χ 1偏好性的变化观察了薄片。发现其它侧链二面角（χ 2、χ 3、χ 4）受主链影响。本文提出了更准确的分布，侧链二面角，这是从增加的蛋白质数量确定到高分辨率。根据主链的二级结构给出了所有残基的χ 1和χ 2角的平均值和标准偏差。对于其中χ 3和χ 4旋转影响C原子位置的侧链的最流行构象给出平均值和标准偏差。
The relationship between the preferred side-chain dihedral angles and the secondary structure of a residue was examined. The structures of 61 proteins solved to a resolution of 2.0 .ANG. (1 .ANG. = 0.1 nm) or better were analysed using a relational database to store the information. The strongest feature observed was that the .chi.1 distribution for most side-chains in an .alpha.-helix showed an absence of the g- conformation and a shift towards the t conformation when compared to the non-.alpha./.beta. structures. The exceptions to this tendency were for short polar side-chains that form hydrogen bonds with the main-chain which prefer g+. shifts in the .chi.1 preferences for residues in the .beta.-sheet were observed. Other side-chain dihedral angles (.chi.2, .chi.3, .chi.4) were found to be influenced by the main-chain. This paper presents more accurate distributions for the side-chain dihedral angles which were obtained from the increased number of proteins determined to high resolution. The means and standard deviations for .chi.1 and .chi.2 angles are presented for all residues according to the secondary structure of the main-chain. The means and standard deviations are given for the most popular conformations for side-chains in which .chi.3 and .chi.4 rotations affect the position of C atoms.