Physical basis for characterizing native structures of proteins
Physical basis for characterizing native structures of proteins
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DOI：
10.1016/j.cplett.2007.01.087
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发表时间：
2007-03-22
影响因子：
2.8
通讯作者：
Kinoshita, Masahiro
中科院分区：
文献类型：
--
作者：
Harano, Yuichi;Roth, Roland;Kinoshita, Masahiro
我们认为蛋白质折叠的主要驱动力是水熵的增加。分子内氢的形成。键的重要性仅仅在于在折叠过程中尽可能地减少脱水损失。聚焦这两个因素的物理基础上，我们构建了一个新的能量函数，这是相当迅速地使用我们的形态计量方法计算。选择七种不同的蛋白质，并考虑每种蛋白质的天然折叠和超过600个错误折叠结构。它表明，能量函数总是最低的天然结构。(c)2007 Elsevier B.V.保留所有权利。
We argue that the major driving force in protein folding is a gainin the water entropy. The formation of intramolecular hydrogen. bonds is important just for reducing the dehydration penalty as much as possible during the folding process. Focusing the physical basis on these two factors, we construct a new energy function which is calculated quite rapidly using our morphometric approach. Seven different proteins are chosen, and the native fold and over 600 misfolded structures are considered for each protein. It is shown that the energy function is always the lowest for the native structure. (c) 2007 Elsevier B.V. All rights reserved.