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100 1 _ |a Kämpf, Kerstin
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245 _ _ |a Quasielastic neutron scattering studies on couplings of protein and water dynamics in hydrated elastin
260 _ _ |a Melville, NY
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|b American Institute of Physics
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520 _ _ |a 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.
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650 1 7 |a Polymers, Soft Nano Particles and Proteins
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693 _ _ |a Forschungs-Neutronenquelle Heinz Maier-Leibnitz
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700 1 _ |a Demuth, Dominik
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700 1 _ |a Zamponi, Michaela
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700 1 _ |a Wuttke, Joachim
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700 1 _ |a Vogel, Michael
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773 _ _ |a 10.1063/5.0011107
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856 4 _ |y Published on 2020-06-30. Available in OpenAccess from 2021-06-30.
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856 4 _ |y Published on 2020-06-30. Available in OpenAccess from 2021-06-30.
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