Home > Publications database > Quasielastic neutron scattering studies on couplings of protein and water dynamics in hydrated elastin |
Journal Article | FZJ-2020-02445 |
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2020
American Institute of Physics
Melville, NY
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Please use a persistent id in citations: http://hdl.handle.net/2128/25342 doi:10.1063/5.0011107
Abstract: erforming quasielastic neutron scattering measurements and analyzing both elastic and quasielasic contributions, we study protein and water dynamics of hydrated elastin. At low temperatures, hydration-independent methyl group rotation dominates the findings. It is characterized by a Gaussian distribution of activation energies centered at about Em = 0.17 eV. At ∼195 K, coupled protein–water motion sets in. The hydration water shows diffusive motion, which is described by a Gaussian distribution of activation energies with Em = 0.57 eV. This Arrhenius behavior of water diffusion is consistent with previous results for water reorientation, but at variance with a fragile-to-strong crossover at ∼225 K. The hydration-related elastin backbone motion is localized and can be attributed to the cage rattling motion. We speculate that its onset at ∼195 K is related to a secondary glass transition, which occurs when a β relaxation of the protein has a correlation time of τβ ∼ 100 s. Moreover, we show that its temperature-dependent amplitude has a crossover at the regular glass transition Tg = 320 K of hydrated elastin, where the α relaxation of the protein obeys τα ∼ 100 s. By contrast, we do not observe a protein dynamical transition when water dynamics enters the experimental time window at ∼240 K.
Keyword(s): Polymers, Soft Nano Particles and Proteins (1st) ; Condensed Matter Physics (2nd) ; Biology (2nd)
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