A broad glass transition in hydrated proteins |
| |
Authors: | S Khodadadi A MalkovskiyA Kisliuk AP Sokolov |
| |
Institution: | Department of Polymer Science, University of Akron, Akron, OH 44325, USA |
| |
Abstract: | We performed Raman and Brillouin scattering measurements to estimate glass transition temperature, Tg, of hydrated protein. The measurements reveal very broad glass transition in hydrated lysozyme with approximate Tg ∼ 180 ± 15 K. This result agrees with a broad range of Tg ∼ 160–200 K reported in literature for hydrated globular proteins and stresses the difference between behavior of hydrated biomolecules and simple glass-forming systems. Moreover, the main structural relaxation of the hydrated protein system that freezes at Tg ∼ 180 K remains unknown. We emphasize the difference between the “dynamic transition”, known as a sharp rise in mean-squared atomic displacement <r2> at temperatures around TD ∼ 200–230 K, and the glass transition. They have different physical origin and should not be confused. |
| |
Keywords: | Hydrated protein Glass transition temperature Dynamic transition Light scattering Dielectric spectroscopy |
本文献已被 ScienceDirect 等数据库收录! |
|