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


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.

Publication DOI:
Divisions: College of Engineering & Physical Sciences > Systems analytics research institute (SARI)
College of Engineering & Physical Sciences > School of Computer Science and Digital Technologies > Applied Mathematics & Data Science
Additional Information: © 2017, Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
Uncontrolled Keywords: Electronic, Optical and Magnetic Materials,Atomic and Molecular Physics, and Optics,Condensed Matter Physics,Spectroscopy,Physical and Theoretical Chemistry,Materials Chemistry
Publication ISSN: 1873-3166
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Related URLs: http://www.scop ... tnerID=8YFLogxK (Scopus URL)
PURE Output Type: Article
Published Date: 2017-06
Published Online Date: 2017-01-07
Accepted Date: 2017-01-06
Submitted Date: 2016-10-13
Authors: Atamas, N.
Bardik, V.
Bannikova, A.
Grishina, O.
Lugovskoi, E.
Lavoryk, S.
Makogonenko, Y.
Korolovych, V.
Nerukh, D. (ORCID Profile 0000-0001-9005-9919)
Paschenko, V.

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