alpha-Helix dipole model and electrostatic stabilization of 4-alpha-helical proteins.
alpha-Helix dipole model and electrostatic stabilization of 4-alpha-helical proteins.
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α-螺旋偶极子模型和 4-α-螺旋蛋白的静电稳定。
DOI：
10.1073/pnas.79.15.4545
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发表时间：
1982
影响因子：
11.1
通讯作者：
Salemme,FR
中科院分区：
文献类型：
--
作者：
Sheridan,RP;Levy,RM;Salemme,FR
本文提出了一个简单的偶极模型来计算蛋白质中α-螺旋之间的静电相互作用能。这个模型是用来估计在一个经常性的蛋白质三级结构基序，一个阵列的四个紧密包装的α-螺旋的静电稳定。发现对于所检测的蛋白质（细胞色素c ′、血红蛋白、肌血红蛋白、细胞色素b562和T4噬菌体溶菌酶结构域），它们的相邻螺旋的共同反平行排列赋予5- 7 kcal/mol（1 cal = 4.18 J）的稳定性。相比之下，平行螺旋的类似堆积阵列相对不稳定20千卡/摩尔。这些结果表明，螺旋偶极相互作用是重要的，在这个结构基序的稳定。这些影响都在4-α-螺旋蛋白质的折叠途径和更高的聚集体的稳定性的背景下进行了讨论。
A simple dipole model is developed for estimation of the electrostatic interaction energy between alpha-helices in proteins. This model is used to estimate the electrostatic stabilization in a recurrent protein tertiary structural motif, an array of four closely packed alpha-helices. It is found that, for the proteins examined (cytochrome c', hemerythrin, myohemerythrin, cytochrome b562, and a T4 phage lysozyme domain), their common antiparallel arrangement of adjacent helices confers a stabilization of 5--7 kcal/mol (1 cal = 4.18 J). In contrast, a similarly packed array of parallel helices is relatively destabilized by 20 kcal/mol. These results show that helix-dipole interactions are important in the stabilization of this structural motif. These effects are discussed both in the context of folding pathways for 4-alpha-helical proteins and the stabilization of the higher aggregates.