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.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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