Localizing frustration in native proteins and protein assemblies
Localizing frustration in native proteins and protein assemblies
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DOI：
10.1073/pnas.0709915104
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发表时间：
2007-12-11
影响因子：
11.1
通讯作者：
Wolynes, Peter G.
中科院分区：
文献类型：
--
作者：
Ferreiro, Diego U.;Hegler, Joseph A.;Wolynes, Peter G.
我们提出了一种方法，量化的挫折程度表现在蛋白质生物分子的空间局部相互作用。这种局部化方法平滑地推广了能量景观被漏斗到原生状态的全局标准，这符合最小挫折原则。对结构数据库的调查表明，天然蛋白质是由一个局部相互作用的网络多重连接起来的，这些相互作用单独地受到最小的阻碍。相比之下，发现高度受挫的相互作用聚集在表面上，通常靠近结合位点。这些结合位点在复合物形成后变得不那么受阻碍。
We propose a method of quantifying the degree of frustration manifested by spatially local interactions in protein biomolecules. This method of localization smoothly generalizes the global criterion for an energy landscape to be funneled to the native state, which is in keeping with the principle of minimal frustration. A survey of the structural database shows that natural proteins are multiply connected by a web of local interactions that are individually minimally frustrated. In contrast, highly frustrated interactions are found clustered on the surface, often near binding sites. These binding sites become less frustrated upon complex formation.