Low-temperature librations and dynamical transition in proteins at differing hydration levels

Q2 Biochemistry, Genetics and Molecular Biology Biomolecular Concepts Pub Date : 2022-01-01 DOI:10.1515/bmc-2022-0007
Erika Aloi, R. Bartucci, R. Guzzi
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Abstract

Abstract Hydration of water affects the dynamics and in turn the activity of biomacromolecules. We investigated the dependence of the librational oscillations and the dynamical transition on the hydrating conditions of two globular proteins with different structure and size, namely β-lactoglobulin (βLG) and human serum albumin (HSA), by spin-label electron paramagnetic resonance (EPR) in the temperature range of 120–270 K. The proteins were spin-labeled with 5-maleimide spin-label on free cysteins and prepared in the lyophilized state, at low (h = 0.12) and full (h = 2) hydration levels in buffer. The angular amplitudes of librations are small and almost temperature independent for both lyophilized proteins. Therefore, in these samples, the librational dynamics is restricted and the dynamical transition is absent. In the small and compact beta-structured βLG, the angular librational amplitudes increase with temperature and hydrating conditions, whereas hydration-independent librational oscillations whose amplitudes rise with temperature are recorded in the large and flexible alpha-structured HSA. Both βLG and HSA at low and fully hydration levels undergo the dynamical transition at about 230 K. The overall results indicate that protein librational dynamics is activated at the low hydration level h = 0.12 and highlight biophysical properties that are common to other biosamples at cryogenic temperatures.
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蛋白质在不同水合水平下的低温振动和动力学转变
摘要水的水合作用影响生物大分子的动力学,进而影响其活性。在120–270的温度范围内,我们用自旋标记电子顺磁共振(EPR)研究了两种不同结构和大小的球状蛋白,即β-乳球蛋白(βLG)和人血清白蛋白(HSA)的平动振荡和动力学转变对水合条件的依赖性 K.用游离半胱氨酸上的5-马来酰亚胺自旋标记物对蛋白质进行自旋标记,并在缓冲液中以低(h=0.12)和完全(h=2)水合水平在冻干状态下制备蛋白质。两种冻干蛋白质的平动角振幅都很小,几乎与温度无关。因此,在这些样品中,平动动力学是受限制的,并且不存在动力学跃迁。在小而紧凑的β结构βLG中,角振动振幅随着温度和水合条件而增加,而振幅随着温度而增加的与水合无关的振动振荡记录在大而灵活的α结构HSA中。βLG和HSA在低水化和完全水化水平下都在230左右发生动力学转变 K.总体结果表明,蛋白质库动力学在低水合水平h=0.12下被激活,并突出了在低温下其他生物样品常见的生物物理特性。
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来源期刊
Biomolecular Concepts
Biomolecular Concepts Biochemistry, Genetics and Molecular Biology-Biochemistry, Genetics and Molecular Biology (all)
CiteScore
5.30
自引率
0.00%
发文量
27
审稿时长
12 weeks
期刊介绍: BioMolecular Concepts is a peer-reviewed open access journal fostering the integration of different fields of biomolecular research. The journal aims to provide expert summaries from prominent researchers, and conclusive extensions of research data leading to new and original, testable hypotheses. Aspects of research that can promote related fields, and lead to novel insight into biological mechanisms or potential medical applications are of special interest. Original research articles reporting new data of broad significance are also welcome. Topics: -cellular and molecular biology- genetics and epigenetics- biochemistry- structural biology- neurosciences- developmental biology- molecular medicine- pharmacology- microbiology- plant biology and biotechnology.
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