Denatured state effects and the origin of nonclassical φ values in protein folding
Denatured state effects and the origin of nonclassical φ values in protein folding
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DOI：
10.1021/ja0669878
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发表时间：
2006-12-27
影响因子：
15
通讯作者：
Raleigh, Daniel P.
中科院分区：
文献类型：
--
作者：
Cho, Jae-Hyun;Raleigh, Daniel P.
分析蛋白质折叠的过渡态是了解蛋白质折叠过渡态的最有力的工具之一。原则上，期望Δ k值落在0至1的范围内。然而，已经观察到显著数量的小于0或大于1的λ值。这种非经典值的起源，有时被称为非经典或非经典的非经典值，一直有争议。在这里，我们表明，变性状态能量的突变效应，可以导致非经典的dielectric值。
Analysis of the ϕ value is one of the most powerful tools to understand the transition state for protein folding. In principle, ϕ values are expected to fall in the range of 0 to 1. However, a noticeable number of ϕ values have been observed which are either less than 0 or greater than 1. The origin of such ϕ values, sometimes referred to as noncanonical or nonclassical ϕ values, has been controversial. Here we show that mutational effects upon denatured state energetics can lead to nonclassical ϕ values.