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Number of results
2008 | 114 | 2 | 447-454
Article title

The SAXS and Rheological Studies of HEWL Amyloid Formation

Content
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EN
Abstracts
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.
Keywords
EN
Publisher

Year
Volume
114
Issue
2
Pages
447-454
Physical description
Dates
published
2008-08
received
2007-09-24
Contributors
author
  • Department of Molecular Biophysics, A. Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland
author
  • Department of Molecular Biophysics, A. Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland
author
  • Institute of Acoustics, A. Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland
author
  • Department of Macromolecular Physics, A. Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-appv114n216kz
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