The SAXS and Rheological Studies of HEWL Amyloid Formation

• Authors: A. Szymańska , G. Ślósarek , T. Hornowski , M. Kozak
• Languages of publication: 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

61.05.cf; 87.14.E-

Discipline

• 87.14.E-: Proteins
• 61.05.cf: X-ray scattering (including small-angle scattering)

• Publisher: Institute of Physics, Polish Academy of Sciences
• Journal: Acta Physica Polonica A
• Year: 2008
• Volume: 114
• Issue: 2
• Pages: 447-454

Dates

published

2008-08

received

2007-09-24

Contributors

author

A. Szymańska

• Department of Molecular Biophysics, A. Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland

author

G. Ślósarek

• Department of Molecular Biophysics, A. Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland

author

T. Hornowski

• Institute of Acoustics, A. Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland

author

M. Kozak

• Department of Macromolecular Physics, A. Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland

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Identifiers

DOI

10.12693/APhysPolA.114.447