Water and lysozyme: Some results from the bending and stretching vibrational modes
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11467_2015_Article_488.pdf
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Author(s)
Mallamace, Francesco
Corsaro, Carmelo
Mallamace, Domenico
Vasi, Cirino
Cicero, Nicola
Stanley, H. Eugene
Date Issued
December 2015
Journal
Frontiers of Physics
Publisher
Higher Education Press
Citation
Mallamace, Francesco et al. “Water and Lysozyme: Some Results from the Bending and Stretching Vibrational Modes.” Frontiers of Physics 10.5 (2015): n. pag.
Version
Author's final manuscript
Abstract
The dynamic or glass transition in biomolecules is important to their functioning. Also essential is the transition between the protein native state and the unfolding process. To better understand these transitions, we use Fourier transform infrared spectroscopy to study the vibrational bending and stretching modes of hydrated lysozymes across a wide temperature range. We find that these transitions are triggered by the strong hydrogen bond coupling between the protein and hydration water. More precisely, we demonstrate that in both cases the water properties dominate the evolution of the system. We find that two characteristic temperatures are relevant: in the supercooled regime of confined water, the fragile-to-strong dynamic transition occurs at T[subscript L], and in the stable liquid phase, T* ≈ 315 ± 5 K characterizes the behavior of both isothermal compressibility K[subscript T] (T,P) and the coefficient of thermal expansion a[subscript P] (T,P).
MIT Department
Massachusetts Institute of Technology. Department of Nuclear Science and Engineering
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1007/s11467-015-0488-7
