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Influence of Intermolecular Dipolar Interaction on Spin-Lattice Relaxation of the Three-Proton Group

100%
Ślósarek G.
Acta Physica Polonica A
|
1991
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vol. 79
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issue 5
739-743
EN
Spin-lattice relaxation of a system of three-proton group and a single, motionless spin is analysed. Only the dipole-dipole interaction is taken into account. The mathematical description is compared with the previous results known from literature.
2
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Light Scattering Studies of Hydration and Structural Transformations of Lysozyme

63%
Szymańska A., Ślósarek G.
Acta Physica Polonica A
|
2012
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vol. 121
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issue 3
694-698
EN
We have applied the method of dynamic light scattering to analyse the lysozyme-ethanol interaction. For low ethanol concentration (below 4.3% (v/v)) no chemical denaturation process is observed. When the ethanol concentration grows above the triggering concentration the hydrodynamic radius of lysozyme increases, indicating the structural changes within the protein molecule. The observed structural modifications are attributed to dehydration and preliminary tertiary structure modification of the protein molecule.
3
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The SAXS and Rheological Studies of HEWL Amyloid Formation

51%
Szymańska A., Ślósarek G., Hornowski T., Kozak M.
Acta Physica Polonica A
|
2008
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vol. 114
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issue 2
447-454
EN
We performed small angle X-ray scattering and rheological experiments in order to analyze the aggregation and denaturation processes of hen egg white lysozyme initiated by the presence of ethanol molecule. At low ethanol concentrations (below 60% (v/v)) we did not observe any change of the radius of gyration of lysozyme and no drastic changes in viscosity of the protein solution. With the increase in ethanol concentration up to the final concentration of 85% (v/v) the viscosity of protein solution dramatically increased. For high ethanol concentration a pseudoplastic behavior of lysozyme solution was observed, indicating a process of aggregation and reorientation of the protein molecules. Similar effects were observed in small angle X-ray scattering experiments. We assume that the analysis of the aggregation processes of the hen egg white lysozyme could contribute to our understanding of the mechanism of lysozyme amyloid formation.
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