A broad glass transition in hydrated proteins

S. Khodadadi; A. Malkovskiy; A. Kisliuk; A. P. Sokolov

doi:10.1016/j.bbapap.2009.05.006

A broad glass transition in hydrated proteins

S. Khodadadi, A. Malkovskiy, A. Kisliuk, A. P. Sokolov

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81 Scopus citations

Abstract

We performed Raman and Brillouin scattering measurements to estimate glass transition temperature, T_g, of hydrated protein. The measurements reveal very broad glass transition in hydrated lysozyme with approximate T_g ∼ 180 ± 15 K. This result agrees with a broad range of T_g ∼ 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 T_g ∼ 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 T_D ∼ 200-230 K, and the glass transition. They have different physical origin and should not be confused.

Original language	English
Pages (from-to)	15-19
Number of pages	5
Journal	Biochimica et Biophysica Acta - Proteins and Proteomics
Volume	1804
Issue number	1
DOIs	https://doi.org/10.1016/j.bbapap.2009.05.006
State	Published - Jan 2010

Funding

We thank R. Gregory and S. Azzam for their help with the sample preparation and acknowledge financial support from the NSF Polymer program (DMR-0804571).

Keywords

Dielectric spectroscopy
Dynamic transition
Glass transition temperature
Hydrated protein
Light scattering

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10.1016/j.bbapap.2009.05.006

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N2 - 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 2> at temperatures around TD ∼ 200-230 K, and the glass transition. They have different physical origin and should not be confused.

AB - 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 2> at temperatures around TD ∼ 200-230 K, and the glass transition. They have different physical origin and should not be confused.

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A broad glass transition in hydrated proteins

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