All-atom contact potential approach to protein thermostability analysis
All-atom contact potential approach to protein thermostability analysis
复制标题
DOI：
10.1002/bip.20600
复制
发表时间：
2007-01-01
期刊：
影响因子：
2.9
通讯作者：
Xiao, Yi
中科院分区：
文献类型：
--
作者：
Chen, Changjun;Li, Lin;Xiao, Yi
在本文中，我们使用全原子势能来定义和分析中温和嗜热蛋白质中的残基间接触。选择了15个蛋白质家族，每个家族有两个具有代表性的蛋白质，它们的偏好环境温度差异很大。我们发现，与以前使用的其他因素相比，以这种方式定义的接触的数量和能量与蛋白质的首选温度显示出更强的相关性。我们还发现，带电-极性和带电-非极性残基接触不仅具有较大的接触数，而且具有较低的单次接触能。此外，最重要的是，与中温蛋白相比，大多数嗜热蛋白具有更多的带电-极性和带电-非极性残基接触。这表明，它们可能在蛋白质的热稳定性中发挥重要作用，除了通常的带电和非极性-非极性残基接触。带电残基不仅与其他带电残基形成接触，而且与极性或非极性残基形成接触，从而进一步增强接触网络的强度，进而提高蛋白质的热稳定性，从而对蛋白质产生深远的影响。(C)2006年威利期刊公司。
In this paper we use all-atom potential energy to define and analyze the inter-residue contacts in mesophilic and thermophilic proteins. Fifteen families of proteins are selected and each family has two representative proteins with greatly different preferred environmental temperatures. We find that both the number and energy of the contacts defined in this way show stronger correlations with the preferred temperatures of proteins than other factors used before. We also find that the charged-polar and charged-nonpolar residue contacts not only have larger contact numbers but also have lower single contact energies. Furthermore the most important is that most of the thermophilic proteins have more charged-polar and charged-nonpolar residue contacts than their mesophilic counterparts. This suggests that they may play an important role in the thermostability of proteins, except usual charged-charged and nonpolar-nonpolar residue contacts. Charged residues may exert their profound influence by forming contacts not only with other charged residues but also with polar or nonpolar residues, thus further increasing the strength of contact network and then the thermostability of proteins. (c) 2006 Wiley Periodicals, Inc.