Autor: Szymańska, G. - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Light Scattering Studies of Hydration and Structural Transformations of Lysozyme
Autorzy:: Szymańska, A.
Ślósarek, G.
Powiązania:: https://bibliotekanauki.pl/articles/1489917.pdf
Data publikacji:: 2012-03
Wydawca:: Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:: 87.15.kr
34.50.-s
Opis:: 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.
Źródło:: Acta Physica Polonica A; 2012, 121, 3; 694-698
0587-4246
1898-794X
Pojawia się w:: Acta Physica Polonica A
Dostawca treści:: Biblioteka Nauki

Artykuł

Skocz do pozycji: 2.

Tytuł:: The SAXS and Rheological Studies of HEWL Amyloid Formation
Autorzy:: Szymańska, A.
Ślósarek, G.
Hornowski, T.
Kozak, M.
Powiązania:: https://bibliotekanauki.pl/articles/1812257.pdf
Data publikacji:: 2008-08
Wydawca:: Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:: 61.05.cf
87.14.E-
Opis:: 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.
Źródło:: Acta Physica Polonica A; 2008, 114, 2; 447-454
0587-4246
1898-794X
Pojawia się w:: Acta Physica Polonica A
Dostawca treści:: Biblioteka Nauki

Artykuł

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