Water and lysozyme: Some results from the bending and stretching vibrational modes
Author(s)Mallamace, Francesco; Corsaro, Carmelo; Mallamace, Domenico; Vasi, Cirino; Cicero, Nicola; Stanley, H. Eugene; ... Show more Show less
MetadataShow full item record
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).
DepartmentMassachusetts Institute of Technology. Department of Nuclear Science and Engineering
Frontiers of Physics
Higher Education Press
Mallamace, Francesco et al. “Water and Lysozyme: Some Results from the Bending and Stretching Vibrational Modes.” Frontiers of Physics 10.5 (2015): n. pag.
Author's final manuscript