Gudiksen Katherine L, Gitlin Irina, Whitesides George M
Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.
Proc Natl Acad Sci U S A. 2006 May 23;103(21):7968-72. doi: 10.1073/pnas.0602816103. Epub 2006 May 12.
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 SDS, 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 SDS, and in the profiles of the denaturation pathways. We also demonstrate that these differences can be exploited in the analysis of mixtures.
本文表明,蛋白质在含有中等浓度(0.1 - 10 mM)十二烷基硫酸钠(SDS)的缓冲液中表现出意想不到的广泛行为(完全展开、形成稳定的中间状态、与SDS特异性结合以及各种动力学现象);毛细管电泳提供了一种检测这些行为的便捷方法。对蛋白质对SDS反应动力学的研究为区分和表征蛋白质提供了一种途径。基于对18种不同蛋白质的研究,我们证明了蛋白质在使其变性的SDS浓度、在SDS中的展开速率以及变性途径的轮廓方面存在差异。我们还证明了这些差异可用于混合物分析。