TY - JOUR
T1 - The effect of water dynamics on conformation changes of albumin in pre-denaturation state
T2 - photon correlation spectroscopy and simulation
AU - Atamas, N.
AU - Bardik, V.
AU - Bannikova, A.
AU - Grishina, O.
AU - Lugovskoi, E.
AU - Lavoryk, S.
AU - Makogonenko, Y.
AU - Korolovych, V.
AU - Nerukh, D.
AU - Paschenko, V.
N1 - © 2017, Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/
PY - 2017/6
Y1 - 2017/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85011409218&partnerID=8YFLogxK
U2 - 10.1016/j.molliq.2017.01.017
DO - 10.1016/j.molliq.2017.01.017
M3 - Article
SN - 0167-7322
VL - 235
SP - 17
EP - 23
JO - Journal of Molecular Liquids
JF - Journal of Molecular Liquids
ER -