蛋白质对进化突变稳定性的拟议机制。
Proposed mechanism for stability of proteins to evolutionary mutations.
作者信息
Nelson E D, Onuchic J N
机构信息
Departments of Chemistry and Physics, University of California at San Diego, La Jolla, CA 92093, USA.
出版信息
Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10682-6. doi: 10.1073/pnas.95.18.10682.
Abstract
It is shown that the sequence-ordering tendencies induced by design into different fast-folding, thermally stable native structures interfere. This interference results in a type of quasiorthogonality between optimal native structures, which divides sequence space into fast-folding, thermally stable families surrounded by slow-folding, low stability shells. A concrete example of this effect is provided by using a simple alpha carbon type model in which a complete correspondence is established between sequence and structure. It is speculated that gaps can occur in the space of protein-like sequences separating the sequence families and resulting in a mechanism for stability and diversity of protein sequence information.
摘要
研究表明，设计引入不同快速折叠、热稳定天然结构中的序列排序倾向会相互干扰。这种干扰导致了最优天然结构之间的一种准正交性，它将序列空间划分为被缓慢折叠、低稳定性外壳包围的快速折叠、热稳定家族。通过使用一个简单的α-碳类型模型提供了这种效应的具体例子，其中在序列和结构之间建立了完全对应关系。据推测，在分离序列家族的类蛋白质序列空间中可能会出现间隙，从而产生一种蛋白质序列信息稳定性和多样性的机制。
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