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首页> 外文期刊>Physical chemistry chemical physics: PCCP >NMR studies on hydrophobic interactions in solution - Part 5. Effect of urea on the hydrophobic self-association of tert-butanol in water at different temperatures
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NMR studies on hydrophobic interactions in solution - Part 5. Effect of urea on the hydrophobic self-association of tert-butanol in water at different temperatures

机译：溶液中疏水相互作用的NMR研究-第5部分。脲对不同温度下水中叔丁醇的疏水自缔合的影响

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An NMR A(22) parameter study of the effect of urea on the hydrophobic self-association of tert-butanol in aqueous solutions is presented. One aim of the present paper is to contribute to the understanding of the urea effect in protein denaturation. The experimental data used for the computation of the A(22) parameters, namely the self-diffusion coefficients and the intermolecular H-1 relaxation rates of tert-butanol in the ternary system, together with the additionally measured self-diffusion coefficients of water, are also examined with respect to a possible structure-breaking effect of urea on the aqueous phase which has been discussed in the literature. We obtain the remarkable result that in a certain mixture range addition of urea can increase the translational mobility of the solute tert-butanol, whereas it always decreases the mobility of bulk water. Thus, we could not detect a structure-breaking effect of urea on the aqueous phase. The urea content was varied up to 12 mol% in the temperature range 10-40 degrees C. It is found that low urea concentrations enhance the hydrophobic self-association in the water-rich region in the whole temperature range. With low tert-butanol concentrations this enhancement effect reaches a pronounced maximum. At higher urea concentrations a destabilisation of the hydrophobic interaction is observed. This latter result is in agreement with the need for relatively high urea concentrations to achieve protein denaturation. Obviously, the same basic mechanism controls the effect of urea not only on the stability of hydrophobic association of comparatively small molecules but also on the conformation of large biomolecules. [References: 37]
机译：提出了NMR A（22）参数研究尿素对叔丁醇在水溶液中的疏水自缔合的影响。本文的目的之一是有助于理解蛋白质变性中的尿素作用。用于计算A（22）参数的实验数据，即三元体系中叔丁醇的自扩散系数和分子间H-1弛豫速率，以及另外测得的水的自扩散系数，还针对尿素对水相的可能的结构破坏作用进行了研究，这已经在文献中进行了讨论。我们获得了显着的结果，在一定的混合范围内添加尿素可以提高溶质叔丁醇的平移迁移率，而它总是降低散装水的迁移率。因此，我们无法检测到尿素对水相的破坏结构作用。在10-40℃的温度范围内，尿素含量变化至高达12mol％。发现低尿素浓度在整个温度范围内增强了富水区域中的疏水性自缔合。在叔丁醇浓度低的情况下，这种增强作用达到了明显的最大值。在较高的尿素浓度下，观察到疏水相互作用的不稳定。后一结果与需要相对较高的尿素浓度以实现蛋白质变性相一致。显然，相同的基本机理不仅控制尿素对较小分子疏水缔合的稳定性，而且对大生物分子构象的控制。 [参考：37]

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