球状蛋白质中序列与构象关系的编码分析。主链链段中转角和扭结处残基对的分布。
Analysis of the code relating sequence to conformation in globular proteins. The distribution of residue pairs in turns and kinks in the backbone chain.
作者信息
Robson B, Pain R H
出版信息
Biochem J. 1974 Sep;141(3):899-904. doi: 10.1042/bj1410899.
Abstract
- The residue pair is considered as the fundamental unit which differentiates alpha-helix, beta-pleated sheet and the various turns and kink structures of the protein backbone. 2. The HPLG alphabet (Robson & Pain, 1974) is used to group pairs of residues, giving 16 possible conformational pairs, all of which are found with differing frequencies in the nine proteins examined. 3. The frequencies of occurrence of the 16 different types of turn or kink are analysed in relation to the constituent amino acids. Those containing the L or G conformation are of low frequency and are grouped for purposes of this analysis. 4. The distribution of amino acids within all the conformational pairs is non-random, with distinct preferences shown by certain residues. 5. All pairs containing an L or G conformation require the presence of a glycine or a proton-donor side chain. 6. The results are discussed in terms of the determination of these ;random' structures by local interactions.
摘要
- 残基对被视为区分α螺旋、β折叠以及蛋白质主链各种转角和扭结结构的基本单元。2. 使用HPLG字母表（罗布森和佩恩，1974年）对残基对进行分组，得到16种可能的构象对，在检测的9种蛋白质中，所有这些构象对出现的频率各不相同。3. 分析了16种不同类型转角或扭结的出现频率与组成氨基酸的关系。那些含有L或G构象的频率较低，为便于分析将它们归为一组。4. 所有构象对中氨基酸的分布并非随机，某些残基表现出明显的偏好。5. 所有含有L或G构象的对都需要有甘氨酸或质子供体侧链存在。6. 根据通过局部相互作用确定这些“随机”结构的情况对结果进行了讨论。
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