O2 migration pathways are not conserved across proteins of a similar fold
O2 migration pathways are not conserved across proteins of a similar fold
复制标题
DOI：
10.1529/biophysj.107.108712
复制
发表时间：
2007-11-01
影响因子：
3.4
通讯作者：
Schulten, Klaus
中科院分区：
文献类型：
--
作者：
Cohen, Jordi;Schulten, Klaus
计算生物学的最新进展使得绘制蛋白质内部气体迁移途径的完整网络和能量分布图成为可能。虽然O-2通路的网络已经在少数蛋白质中被表征，但这些通路的一般性质和位置之前还没有在蛋白质之间进行比较。在这项研究中，计算了12个单体珠蛋白内的O-2通路图。研究发现，尽管所研究的珠蛋白具有保守的三级结构褶皱，但O-2通路网络的形状和拓扑结构在不同的珠蛋白之间表现出很大的可变性，除非两个珠蛋白几乎相同。然而，发现O-2通路的位置与大疏水残基的位置相关，并且在两个不相关的蛋白质家族中观察到类似的相关性：单体珠蛋白和含铜胺氧化酶。这些结果对蛋白质中气体途径的进化和涉及莫迪的蛋白质工程应用具有启示意义。这些途径的阳离子。
Recent advances in computational biology have made it possible to map the complete network and energy profile of gas migration pathways inside proteins. Although networks of O-2 pathways have already been characterized for a small number of proteins, the general properties and locations of these pathways have not been previously compared between proteins. In this study, maps of the O-2 pathways inside 12 monomeric globins were computed. It is found that, despite the conserved tertiary structure fold of the studied globins, the shape and topology of O-2 pathway networks exhibit a large variability between different globins, except when two globins are nearly identical. The locations of the O-2 pathways are, however, found to be correlated with the location of large hydrophobic residues, and a similar correlation is observed in two unrelated protein families: monomeric globins and copper-containing amine oxidases. The results have implications for the evolution of gas pathways in proteins and for protein engineering applications involving modi. cations of these pathways.