S
Sebastian Pawlus
Researcher at University of Silesia in Katowice
Publications - 157
Citations - 3995
Sebastian Pawlus is an academic researcher from University of Silesia in Katowice. The author has contributed to research in topics: Dielectric & Relaxation (physics). The author has an hindex of 30, co-authored 150 publications receiving 3492 citations. Previous affiliations of Sebastian Pawlus include Dow Chemical Company & University of Akron.
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Role of Chemical Structure in Fragility of Polymers: A Qualitative Picture
TL;DR: In this article, the authors present dielectric and mechanical relaxation studies of segmental dynamics in various polymers with different side groups and backbone structures, and show that the flexibility of the side groups relative to the backbone is the most important factor controlling fragility in polymers.
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Electric modulus approach to the analysis of electric relaxation in highly conducting (Na 0.75 Bi 0.25 )(Mn 0.25 Nb 0.75 )O 3 ceramics
TL;DR: In this paper, the electrical properties of disordered perovskite-like ceramics in a wide temperature range were investigated by using the x-ray diffraction analysis.
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Influence of hydration on protein dynamics: combining dielectric and neutron scattering spectroscopy data.
TL;DR: The main dielectric process is ascribed to protein's structural relaxation coupled to hydration water and the slowest process to a larger scale protein's motions, which exhibit a smooth, slightly super-Arrhenius temperature dependence between 300 and 180 K.
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Does the Arrhenius Temperature Dependence of the Johari-Goldstein Relaxation Persist above T g ?
TL;DR: It is shown that the Arrhenius temperature dependence of the beta relaxation time does not persist for temperatures above T(g), consistent with inferences drawn from dielectric relaxation measurements at ambient pressure.
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The origin of the dynamic transition in proteins
Sheila Khodadadi,Sebastian Pawlus,Joon Ho Roh,Garcia Sakai,Eugene Mamontov,Alexei P. Sokolov +5 more
TL;DR: By combining neutron and dielectric spectroscopy data, this work was able to follow protein dynamics over an extremely broad frequency range and shows that there is no sudden change in the dynamics of the protein at temperatures around approximately 200-230 K.