Differentiation of proteins based on characteristic patterns of association and denaturation in solutions of SDS
Differentiation of proteins based on characteristic patterns of association and denaturation in solutions of SDS
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DOI：
10.1073/pnas.0602816103
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发表时间：
2006-05-23
影响因子：
11.1
通讯作者：
Whitesides, George M.
中科院分区：
文献类型：
--
作者：
Gudiksen, Katherine L.;Gitlin, Irina;Whitesides, George M.
本文表明，蛋白质在含有中等（0.1-10 mM） SDS浓度的缓冲液中表现出出乎意料的广泛行为（完全展开，形成稳定的中间状态，与SIDS特异性关联以及各种动力学现象）；毛细管电泳为检测这些行为提供了一种方便的方法。检查蛋白质对SDS反应的动力学提供了一种区分和表征蛋白质的方法。基于对18种不同蛋白质的调查，我们证明了蛋白质在变性时SDS的浓度、在小岛屿发展中展开的速度以及变性途径的概况方面存在差异。我们还证明，这些差异可以利用在混合物的分析。
This paper shows that proteins display an unexpectedly wide range of behaviors in buffers containing moderate (0.1-10 mM) concentrations of SDS (complete unfolding, formation of stable intermediate states, specific association with SIDS, and various kinetic phenomena); capillary electrophoresis provides a convenient method of examining these behaviors. Examination of the dynamics of the response of proteins to SDS offers a way to differentiate and characterize proteins. Based on a survey of 18 different proteins, we demonstrate that proteins differ in the concentrations of SDS at which they denature, in the rates of unfolding in SIDS, and in the profiles of the denaturation pathways. We also demonstrate that these differences can be exploited in the analysis of mixtures.