Water Dynamics at Protein Interfaces: Ultrafast Optical Kerr Effect Study

Mazur, K, Heisler, IA and Meech, SR (2012) Water Dynamics at Protein Interfaces: Ultrafast Optical Kerr Effect Study. The Journal of Physical Chemistry A, 116. pp. 2678-2685. ISSN 1089-5639

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    Abstract

    The behavior of water molecules surrounding a protein can have an important bearing on its structure and function. Consequently, a great deal of attention has been focused on changes in the relaxation dynamics of water when it is located at the protein surface. Here we use the ultrafast optical Kerr effect to study the H-bond structure and dynamics of aqueous solutions of proteins. Measurements are made for three proteins as a function of concentration. We find that the water dynamics in the first solvation layer of the proteins are slowed by up to a factor of 8 in comparison to those in bulk water. The most marked slowdown was observed for the most hydrophilic protein studied, bovine serum albumin, whereas the most hydrophobic protein, trypsin, had a slightly smaller effect. The terahertz Raman spectra of these protein solutions resemble those of pure water up to 5 wt % of protein, above which a new feature appears at 80 cm–1, which is assigned to a bending of the protein amide chain.

    Item Type: Article
    Faculty \ School: Faculty of Science > School of Chemistry
    University of East Anglia > Faculty of Science > Research Groups > Physical and Analytical Chemistry
    Related URLs:
    Depositing User: Deborah Clemitshaw
    Date Deposited: 17 Jan 2012 14:11
    Last Modified: 25 Jul 2018 03:31
    URI: https://ueaeprints.uea.ac.uk/id/eprint/36220
    DOI: 10.1021/jp2074539

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