Issue 34, 2021

Wide-angle X-ray scattering and molecular dynamics simulations of supercooled protein hydration water

Abstract

Understanding the mechanism responsible for the protein low-temperature crossover observed at T ≈ 220 K can help us improve current cryopreservation technologies. This crossover is associated with changes in the dynamics of the system, such as in the mean-squared displacement, whereas experimental evidence of structural changes is sparse. Here we investigate hydrated lysozyme proteins by using a combination of wide-angle X-ray scattering and molecular dynamics (MD) simulations. Experimentally we suppress crystallization by accurate control of the protein hydration level, which allows access to temperatures down to T = 175 K. The experimental data indicate that the scattering intensity peak at Q = 1.54 Å−1, attributed to interatomic distances, exhibits temperature-dependent changes upon cooling. In the MD simulations it is possible to decompose the water and protein contributions and we observe that, while the protein component is nearly temperature independent, the hydration water peak shifts in a fashion similar to that of bulk water. The observed trends are analysed by using the water–water and water-protein radial distribution functions, which indicate changes in the local probability density of hydration water.

Graphical abstract: Wide-angle X-ray scattering and molecular dynamics simulations of supercooled protein hydration water

Supplementary files

Article information

Article type
Paper
Submitted
14 May 2021
Accepted
10 Jul 2021
First published
12 Jul 2021
This article is Open Access
Creative Commons BY-NC license

Phys. Chem. Chem. Phys., 2021,23, 18308-18313

Wide-angle X-ray scattering and molecular dynamics simulations of supercooled protein hydration water

M. Bin, R. Yousif, S. Berkowicz, S. Das, D. Schlesinger and F. Perakis, Phys. Chem. Chem. Phys., 2021, 23, 18308 DOI: 10.1039/D1CP02126E

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. You can use material from this article in other publications, without requesting further permission from the RSC, provided that the correct acknowledgement is given and it is not used for commercial purposes.

To request permission to reproduce material from this article in a commercial publication, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party commercial publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements