由結構推導蛋白質與蛋白質接觸面的動力學特性

Abstract

蛋白質的交互作用完成了許多生物功能。序列研究指出蛋白質與蛋白質作用區富含厭水性胺基酸；然而，目前為止蛋白質的結構資訊尚無法清楚地區分蛋白質與蛋白質的接觸面與其他蛋白質表面。我們在這個研究中分析了兩項與動力學相關的結構資訊: 蛋白質與蛋白質接觸面的中心與蛋白質的質心距離比一般蛋白質表面與蛋白質的質心距離小。蛋白質與蛋白質接觸面的中心的加權接觸數目比一般蛋白質表面的加權接觸數目大。這表示蛋白質與蛋白質接觸面的中心是靠近蛋白質的質量中心並且處於擁擠的堆疊狀態。

Many biological functions result from the interactions between proteins. From sequence information, studies have revealed that the interaction interfaces are conserved in hydrophobic environments. However, structure information is still not clear enough to differentiate interaction interfaces from protein surfaces. In this study, we analyzed two structural properties related to protein dynamics: the core interface residues are closer to the centroid of protein, and the weighted contact numbers of core interface residues are larger than that of surface residues. The results suggest that the core interface residues are nearness to the protein centroid and in a crowded environment.