Thermal characterisation of actin filaments prepared
from adp-actin monomers
被引:0
|
作者:
J. Orbán
论文数: 0引用数: 0
h-index: 0
机构:University of Pécs,Faculty of Medicine, Department of Biophysics
J. Orbán
Kinga Pozsonyi
论文数: 0引用数: 0
h-index: 0
机构:University of Pécs,Faculty of Medicine, Department of Biophysics
Kinga Pozsonyi
Krisztina Szarka
论文数: 0引用数: 0
h-index: 0
机构:University of Pécs,Faculty of Medicine, Department of Biophysics
Krisztina Szarka
Szilvia Barkó
论文数: 0引用数: 0
h-index: 0
机构:University of Pécs,Faculty of Medicine, Department of Biophysics
Szilvia Barkó
Emőke Bódis
论文数: 0引用数: 0
h-index: 0
机构:University of Pécs,Faculty of Medicine, Department of Biophysics
Emőke Bódis
D. Lőrinczy
论文数: 0引用数: 0
h-index: 0
机构:University of Pécs,Faculty of Medicine, Department of Biophysics
D. Lőrinczy
机构:
[1] University of Pécs,Faculty of Medicine, Department of Biophysics
[2] Office for Academy Research
Groups Attached to Universities and other Institutions at University of Pécs,Research Group
for Fluorescence Spectroscopy
来源:
Journal of Thermal Analysis and Calorimetry
|
2006年
/
84卷
The thermodynamic properties of the ADP- and ATP-actin filaments were
compared by the method of differential scanning calorimetry. The lower melting
point for the ADP-F-actin filament (58.4 vs. 64.5°C for ATP-F-actin) indicated
that compared to the ATP-actin filaments its structure was less resistant
to heat denaturation. The detailed thermodynamic characterisation of the proteins
was carried out by the analysis of the calorimetric enthalpy, the entropy
and the free enthalpy changes. All of the determined parameters gave lower
values to the ADP-actin filaments than to the ATP-actin filaments. The calculated
values of the activation energy also demonstrated that compared to the ADP-F-actin
the ATP-F-actin was thermodynamically more resistant to the denaturing effect
of heat.