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内在无序和自缔合对蛋白质平移扩散的影响:以α-酪蛋白为例。

Effect of Intrinsic Disorder and Self-Association on the Translational Diffusion of Proteins: The Case of α-Casein.

作者信息

Melnikova Daria L, Skirda Vladimir D, Nesmelova Irina V

机构信息

Department of Physics, Kazan Federal University , Kazan 420011, Russia.

出版信息

J Phys Chem B. 2017 Apr 13;121(14):2980-2988. doi: 10.1021/acs.jpcb.7b00772. Epub 2017 Mar 31.

Abstract

Translational diffusion is the major mode of macromolecular transport in leaving organisms, and therefore it is vital to many biological and biotechnological processes. Although translational diffusion of proteins has received considerable theoretical and experimental scrutiny, much of that attention has been directed toward the description of globular proteins. The translational diffusion of intrinsically disordered proteins (IDPs), however, is much less studied. Here, we use a pulsed-gradient nuclear magnetic resonance technique (PFG NMR) to investigate the translational diffusion of a disordered protein in a wide range of concentrations using α-casein that belongs to the class of natively disordered proteins as an example.

摘要

平移扩散是大分子在离开生物体时运输的主要方式,因此对许多生物学和生物技术过程至关重要。尽管蛋白质的平移扩散已受到相当多的理论和实验研究,但其中大部分注意力都集中在球状蛋白质的描述上。然而,内在无序蛋白质(IDP)的平移扩散研究得要少得多。在这里,我们以属于天然无序蛋白质类别的α-酪蛋白为例,使用脉冲梯度核磁共振技术(PFG NMR)在广泛的浓度范围内研究无序蛋白质的平移扩散。

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