SPECIFIC RECOGNITION IN THE TERTIARY STRUCTURE OF BETA-SHEETS OF PROTEINS
SPECIFIC RECOGNITION IN THE TERTIARY STRUCTURE OF BETA-SHEETS OF PROTEINS
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DOI：
10.1016/0022-2836(80)90052-2
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发表时间：
1980-01-01
影响因子：
5.6
通讯作者：
SANDER, C
中科院分区：
文献类型：
--
作者：
LIFSON, S;SANDER, C
从30种已知的蛋白质结构中获得相邻反平行（β A）和平行（β P）链上最近邻残基对的出现频率。由于这种配对而产生的链间识别的特异性是β-半乳糖苷酶折叠中的一个因素。表的统计方法进行了研究。对于统计分析来说，足够高计数的残基被单独处理，而其余的残基被组合成具有相似大小、极性和/或遗传交换的小组。个体和小群体之间的特异性识别的假设与广泛的类别（疏水性，中性，极性）的残基之间的非特异性识别的备择假设形成对比。配对相关性的χ 2检验有利于特异性识别而不是非特异性识别，具有高置信度。最大和最显著的相关性是：Ser/Thr（1.9 ± 0.001）。Ile/瓦尔（1.7 ± 0.3）。0.3)和Lys-Arg/Asp-Gln（1.8 ±. 0.3)in β A和Ile/Leu（1.9 ±. 0.4)Gly/Gly对从不出现在任何β-床单。本文推导的特定残基对相关性可用于蛋白质三级结构的统计预测方法。
The frequency of occurrence of nearest neighbor residue pairs on adjacent antiparallel (.beta.A) and parallel (.beta.P) strands is obtained from 30 known protein structures. The specificity of interstrand recognition due to such pairing as a factor in the folding of .beta.-sheets is studied by statistical methods. Residues of sufficiently high count for statistical analysis are treated individually while the rest are combined into small groups of similar size, polarity, and/or genetic exchangeability. The hypothesis of specific recognition between individuals and small groups is contrasted with the alternative hypothesis of nonspecific recognition between broad classes (hydrophobic, neutral, polar) of residues. A .chi.2 test of pair correlations favors specific recognition against nonspecific recognition with a high level of confidence. The largest and most significant correlations are: Ser/Thr (1.9 .+-. 0.3), Ile/Val (1.7 .+-. 0.3) and Lys-Arg/Asp-Gln (1.8 .+-. 0.3) in .beta.A, and Ile/Leu (1.9 .+-. 0.4) in .beta.P. The pair Gly/Gly never occurs in any .beta.-sheet. The specific residue-pair correlations derived here may be useful in statistical prediction methods of protein tertiary structure.