Peculiarities of the Dynamical Hydration Shell of Native Conformation Protein Using a Bovine Serum Albumin Example.

IF 2.2 3区 化学 Q2 INSTRUMENTS & INSTRUMENTATION
Applied Spectroscopy Pub Date : 2024-10-01 Epub Date: 2024-06-17 DOI:10.1177/00037028241261097
Nikita V Penkov
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Abstract

This paper describes an approach based on the method of terahertz time-domain spectroscopy, which allows the analysis of dynamical hydration shells of proteins with a thickness of 1-2 nm. Using the example of bovine serum albumin in three conformations, it is shown that the hydration shells of the protein are characterized by increased binding of water molecules in the primary hydration layers, and in more distant areas of hydration, on the contrary, the water structure is somewhat destroyed. The fraction of free or weakly bound molecules, usually observed in the structure of liquid water in hydration shells, become more numerous but its average binding is greater than in undisturbed water. The energy distribution of hydrogen bonds in hydration shells is narrowed compared to undisturbed water. All these manifestations of hydration are most pronounced for the native conformation of the protein. Also, the hydration shells of the native protein are characterized by a smaller number of hydrogen bonds and a tendency to decrease their average energy compared to non-native conformations. The fact of a pronounced peculiarity of the hydration shells of the protein in the native conformation has been noted for different proteins before. However, the methodological approach used in this work for the first time allowed this peculiarity to be described by specific parameters of the intermolecular structure and dynamics of water.

以牛血清白蛋白为例说明原生构象蛋白质动态水合壳的特殊性。
本文介绍了一种基于太赫兹时域光谱法的方法,该方法可以分析厚度为 1-2 纳米的蛋白质动态水合壳。以三种构象的牛血清白蛋白为例,研究表明蛋白质水合壳的特点是水分子在主要水合层的结合增加,相反,在较远的水合区域,水结构受到一定程度的破坏。通常在水合壳液态水结构中观察到的自由或弱结合分子部分变得更多,但其平均结合力大于未受干扰的水。与未受扰动的水相比,水合壳中氢键的能量分布变窄。所有这些水合现象在蛋白质的原生构象中最为明显。此外,与非原生构象相比,原生蛋白质水合壳的特点是氢键数量较少,平均能量趋于降低。蛋白质在原生构象中的水合壳具有明显的特殊性,这一点以前在不同的蛋白质中都注意到过。不过,这项研究首次采用了分子间结构和水动力学的特定参数来描述这种特殊性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Applied Spectroscopy
Applied Spectroscopy 工程技术-光谱学
CiteScore
6.60
自引率
5.70%
发文量
139
审稿时长
3.5 months
期刊介绍: Applied Spectroscopy is one of the world''s leading spectroscopy journals, publishing high-quality peer-reviewed articles, both fundamental and applied, covering all aspects of spectroscopy. Established in 1951, the journal is owned by the Society for Applied Spectroscopy and is published monthly. The journal is dedicated to fulfilling the mission of the Society to “…advance and disseminate knowledge and information concerning the art and science of spectroscopy and other allied sciences.”
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