Abstract
Protein functional motions are ultimately connected to water dynamics. The goal of this study is to link the conformational dynamics of albumin to a dynamic transition taking place at ∼ 42°C in water. We report the results of dynamic light scattering measurements of albumin aqueous solution in the temperature interval 20-65°C. The processing of the experimental data produced the temperature dependence of the macromolecular hydrodynamic radius. We demonstrate that the growth of the macromolecular size in this temperature range can be divided into two stages that are connected to the dynamical properties of water.
| Original language | English |
|---|---|
| Pages (from-to) | 60-64 |
| Number of pages | 5 |
| Journal | Journal of Molecular Liquids |
| Volume | 176 |
| Early online date | 26 Sep 2012 |
| DOIs | |
| Publication status | Published - Dec 2012 |
| Event | EMLG/JMLG 2011 Annual Meeting 11 - 15 September 2011 - , United Kingdom Duration: 11 Sep 2011 → 15 Nov 2011 |
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Bibliographical note
Selected Papers on Molecular Liquids presented at the EMLG/JMLG 2011 Annual Meeting 11 - 15 September 2011Keywords
- conformational dynamics
- dynamic light scattering
- human serum albumin
- hydrodynamic radius
- hydrogen bonds
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Light scattering study of human serum albumin in pre-denaturation : relation to dynamic transition in water at 42°C. / Bardik, Vitaliy; Gotsulskii, Vladimir; Pavlov, Evgen; Malomuzh, Nikolai; Nerukh, Dmitry; Yanchuk, Igor; Lavoryk, Serhiy.
In: Journal of Molecular Liquids, Vol. 176, 12.2012, p. 60-64.Research output: Contribution to journal › Special issue
TY - JOUR
T1 - Light scattering study of human serum albumin in pre-denaturation
T2 - relation to dynamic transition in water at 42°C
AU - Bardik, Vitaliy
AU - Gotsulskii, Vladimir
AU - Pavlov, Evgen
AU - Malomuzh, Nikolai
AU - Nerukh, Dmitry
AU - Yanchuk, Igor
AU - Lavoryk, Serhiy
N1 - Selected Papers on Molecular Liquids presented at the EMLG/JMLG 2011 Annual Meeting 11 - 15 September 2011
PY - 2012/12
Y1 - 2012/12
N2 - Protein functional motions are ultimately connected to water dynamics. The goal of this study is to link the conformational dynamics of albumin to a dynamic transition taking place at ∼ 42°C in water. We report the results of dynamic light scattering measurements of albumin aqueous solution in the temperature interval 20-65°C. The processing of the experimental data produced the temperature dependence of the macromolecular hydrodynamic radius. We demonstrate that the growth of the macromolecular size in this temperature range can be divided into two stages that are connected to the dynamical properties of water.
AB - Protein functional motions are ultimately connected to water dynamics. The goal of this study is to link the conformational dynamics of albumin to a dynamic transition taking place at ∼ 42°C in water. We report the results of dynamic light scattering measurements of albumin aqueous solution in the temperature interval 20-65°C. The processing of the experimental data produced the temperature dependence of the macromolecular hydrodynamic radius. We demonstrate that the growth of the macromolecular size in this temperature range can be divided into two stages that are connected to the dynamical properties of water.
KW - conformational dynamics
KW - dynamic light scattering
KW - human serum albumin
KW - hydrodynamic radius
KW - hydrogen bonds
UR - http://www.scopus.com/inward/record.url?scp=84870477596&partnerID=8YFLogxK
U2 - 10.1016/j.molliq.2012.09.012
DO - 10.1016/j.molliq.2012.09.012
M3 - Special issue
AN - SCOPUS:84870477596
VL - 176
SP - 60
EP - 64
JO - Journal of Molecular Liquids
JF - Journal of Molecular Liquids
SN - 0167-7322
ER -