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 |
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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Bardik, V., Gotsulskii, V., Pavlov, E., Malomuzh, N., Nerukh, D., Yanchuk, I., & Lavoryk, S. (2012). Light scattering study of human serum albumin in pre-denaturation: relation to dynamic transition in water at 42°C. Journal of Molecular Liquids, 176, 60-64. https://doi.org/10.1016/j.molliq.2012.09.012