The effect of water dynamics on conformation changes of albumin in pre-denaturation state: photon correlation spectroscopy and simulation

N. Atamas, V. Bardik*, A. Bannikova, O. Grishina, E. Lugovskoi, S. Lavoryk, Y. Makogonenko, V. Korolovych, D. Nerukh, V. Paschenko

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Water is essential for protein three-dimensional structure, conformational dynamics, and activity. Human serum albumin (HSA) is one of major blood plasma proteins, and its functioning is fundamentally determined by the dynamics of surrounding water. The goal of this study is to link the conformational dynamics of albumin to the thermal motions in water taking place in the physiological temperature range. We report the results of photon correlation spectroscopy and molecular dynamics simulations of HSA in aqueous solution. The experimental data processing produced the temperature dependence of the HSA hydrodynamic radius and its zeta potential. Molecular dynamics reproduced the results of experiments and revealed changes in the secondary structure caused by the destruction of hydrogen bonds in the macromolecule's globule.
    Original languageEnglish
    Pages (from-to)17-23
    JournalJournal of Molecular Liquids
    Volume235
    Early online date7 Jan 2017
    DOIs
    Publication statusPublished - Jun 2017

    Bibliographical note

    © 2017, Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/

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