Closed loops of nearly standard size: common basic element of protein structure
Closed loops of nearly standard size: common basic element of protein structure
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DOI：
10.1016/s0014-5793(00)01091-7
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发表时间：
2000-01-28
期刊：
影响因子：
3.5
通讯作者：
Trifonov, EN
中科院分区：
文献类型：
--
作者：
Berezovsky, IN;Grosberg, AY;Trifonov, EN
通过筛选晶体蛋白结构数据库中的C α -C α闭合点，得到闭合环的大小分布。该分布在27+/-5残基处最大，真核和原核蛋白也是如此。这显然是蛋白质链轨迹的聚合物统计特性的结果。也就是说，进入循环的闭包取决于链的灵活性（持久性长度）。优选环路尺寸与理论最优环路闭合尺寸一致，检测到的单位大小环路在主要典型褶皱序列上的映射显示环路几乎是规则的紧致连续排列。因此，发现了蛋白质结构的一个新的基本元素；结构多样的特定尺寸的闭环。(C) 2000年欧洲生化学会联合会。
By screening the crystal protein structure database for close C alpha-C alpha contacts, a size distribution of the closed loops is generated. The distribution reveals a maximum at 27+/-5 residues, the same for eukaryotic and prokaryotic proteins. This is apparently a consequence of polymer statistic properties of protein chain trajectory. That is, closure into the loops depends on the flexibility (persistence length) of the chain. The observed preferential loop size is consistent with the theoretical optimal loop closure size, The mapping of the detected unit-size loops on the sequences of major typical folds reveals an almost regular compact consecutive arrangement of the loops. Thus, a novel basic element of protein architecture is discovered; structurally diverse closed loops of the particular size. (C) 2000 Federation of European Biochemical Societies.