Slow dynamics of water molecules on the surface of a globular protein
- 1 January 1996
- journal article
- Published by Royal Society of Chemistry (RSC) in Faraday Discussions
- Vol. 103, 281-294
- https://doi.org/10.1039/fd9960300281
Abstract
Water is essential for the stability and function of biological macromolecules. High-resolution quasi-elastic neutron scattering studies of the translational dynamics of water molecules on the surface of a deuteriated protein are presented. The quasi-elastic spectra from the interfacial H2O are analysed by a confined diffusion model to obtain the elastic incoherent structure factor (EISF), the short-time self-diffusion constant (D) and the residence time, τ0, as functions of coverage and temperature. The combined effects of the hydration level and temperature on the retardation of the single-particle motions are discussed in the light of available NMR relaxation data and of a well known model of α-relaxation from the theory of kinetic glass transitions in dense supercooled fluids. The vibrational density of states of interfacial water is presented as a function of temperature and for two levels of hydration of the protein.Keywords
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