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皮秒时间尺度下蛋白质-水界面的耦合弛豫

Coupled relaxations at the protein-water interface in the picosecond time scale.

作者信息

Paciaroni A, Cornicchi E, Marconi M, Orecchini A, Petrillo C, Haertlein M, Moulin M, Sacchetti F

机构信息

Dipartimento di Fisica, Università degli Studi di Perugia, Via A. Pascoli, I-06123 Perugia, Italy.

出版信息

J R Soc Interface. 2009 Oct 6;6 Suppl 5(Suppl 5):S635-40. doi: 10.1098/rsif.2009.0182.focus. Epub 2009 Jul 29.

Abstract

The spectral behaviour of a protein and its hydration water has been investigated through neutron scattering. The availability of both hydrogenated and perdeuterated samples of maltose-binding protein (MBP) allowed us to directly measure with great accuracy the signal from the protein and the hydration water alone. Both the spectra of the MBP and its hydration water show two distinct relaxations, a behaviour that is reminiscent of glassy systems. The two components have been described using a phenomenological model that includes two Cole-Davidson functions. In MBP and its hydration water, the two relaxations take place with similar average characteristic times of approximately 10 and 0.2 ps. The common time scales of these relaxations suggest that they may be a preferential route to couple the dynamics of the water hydrogen-bond network around the protein surface with that of protein fluctuations.

摘要

通过中子散射研究了蛋白质及其水合水的光谱行为。麦芽糖结合蛋白(MBP)的氢化和全氘代样品的可得性使我们能够非常精确地直接测量仅来自蛋白质和水合水的信号。MBP及其水合水的光谱均显示出两种不同的弛豫,这种行为让人联想到玻璃态系统。使用包含两个科尔 - 戴维森函数的唯象模型描述了这两个组分。在MBP及其水合水中,两种弛豫以相似的平均特征时间发生,分别约为10皮秒和0.2皮秒。这些弛豫的共同时间尺度表明,它们可能是使蛋白质表面周围水氢键网络的动力学与蛋白质涨落的动力学耦合的优先途径。

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Coupled relaxations at the protein-water interface in the picosecond time scale.皮秒时间尺度下蛋白质-水界面的耦合弛豫
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