Evidence of coexistence of change of caged dynamics at Tg and the dynamic transition at Td in solvated proteins

TL;DR

This study demonstrates that solvated proteins exhibit a change in atomic mean square displacements at both the glass transition temperature Tg and the dynamic transition temperature Td, linking protein dynamics to glass-forming behavior.

Contribution

It provides evidence that the change in <u2> at Tg in solvated proteins is analogous to glass-formers, connecting protein dynamics to fundamental glass transition phenomena.

Findings

Change in <u2> observed at Tg in solvated proteins.

Change in <u2> observed at Td in solvated proteins.

Both changes relate to glass-forming behavior and molecular dissipation.

Abstract

Mossbauer spectroscopy and neutron scattering measurements on proteins embedded in solvents including water and aqueous mixtures have emphasized the observation of the distinctive temperature dependence of the atomic mean square displacements, <u2>, commonly referred to as the dynamic transition at some temperature Td. At low temperatures, <u2> increases slowly, but it assume stronger temperature dependence after crossing Td, which depends on the time/frequency resolution of the spectrometer. Various authors have made connection of the dynamics of solvated proteins including the dynamic transition to that of glass-forming substances. Notwithstanding, no connection is made to the similar change of temperature dependence of <u2> obtained by quasielastic neutron scattering when crossing the glass transition temperature Tg, generally observed in inorganic, organic and polymeric glass-formers. Evidences are presented to show that such change of the temperature dependence of <u2> from neutron scattering at Tg is present in hydrated or solvated proteins, as well as in the solvents used unsurprisingly since the latter is just another organic glass-formers. The <u2> obtained by neutron scattering at not so low temperatures has contributions from the dissipation of molecules while caged by the anharmonic intermolecular potential at times before dissolution of cages by the onset of the Johari-Goldstein beta-relaxation. The universal change of <u2> at Tg of glass-formers had been rationalized by sensitivity to change in volume and entropy of the beta-relaxation, which is passed onto the dissipation of the caged molecules and its contribution to <u2>. The same rationalization applies to hydrated and solvated proteins for the observed change of <u2> at Tg.