Berezovsky I N, Grosberg A Y, Trifonov E N
Department of Structural Biology, The Weizmann Institute of Science, Rehovot, Israel.
FEBS Lett. 2000 Jan 28;466(2-3):283-6. doi: 10.1016/s0014-5793(00)01091-7.
By screening the crystal protein structure database for close Calpha-Calpha 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.
通过在晶体蛋白结构数据库中筛选紧密的Cα-Cα接触，生成了闭环的大小分布。该分布显示在27±5个残基处有一个最大值，真核和原核蛋白的情况相同。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，形成环取决于链的柔韧性（持久长度）。观察到的优先环大小与理论上的最佳环闭合大小一致。在主要典型折叠序列上检测到的单位大小环的映射显示，环几乎呈规则紧凑的连续排列。因此，发现了一种新的蛋白质结构基本元件；特定大小的结构多样的闭环。
