Eur. Phys. J. Appl. Phys.
Volume 71, Number 3, September 2015
|Number of page(s)||10|
|Section||Biophysics and Biosensors|
|Published online||14 August 2015|
Biophysical approach to investigate temperature effects on protein dynamics
R & D Group of Biological and Environmental Physics, Department of Physics, Faculty of Science, Mahidol University, 10400 Bangkok, Thailand
2 Rajamangala University of Technology Phra Nakhon, 10800 Bangkok, Thailand
3 Institute for Innovative Learning, Mahidol University, 73170 Nakhon Pathom, Thailand
4 Centre of Excellence in Mathematics, CHE, 328, Si Ayutthaya Road, 10400 Bangkok, Thailand
5 ThEP Center, CHE, 328 Si Ayutthaya Road, 10400 Bangkok, Thailand
6 Department of Chemistry and Center for Innovation in Chemistry, Faculty of Science, Mahidol University, 10400 Bangkok, Thailand
a e-mail: firstname.lastname@example.org
Revised: 11 July 2015
Accepted: 16 July 2015
Published online: 14 August 2015
The main purpose of this work is to gain more understanding of the temperature dependence of Min protein dynamics employing spot tracking technique (STT) and biophysical characterization. We observed and confirmed the variation of protein cluster dynamics at evaluated temperatures. We found that the time MinD was retained at the cell poles played an important role in this variation. From 25 °C to 37 °C, the MinD protein oscillation period decreased 2.3 times and the anomalous dynamic exponent increased 2.4 times. The time-varied anomalous diffusion coefficient was found to be temperature dependent, which was qualitatively consistent with the prediction by Tsallis statistical mechanics. Furthermore, the average apparent effective potential depth of membrane-bound MinD protein decreased from 10.01 to 3.54 kBT. These results showed that the diffusive mode and the MinD protein cluster distribution at the cell poles were altered with temperature and this then affected the whole Min protein dynamics.
© EDP Sciences, 2015
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