<div id="bm-composer-content-wrapper"><div id="bm-composer-content-wrapper" style="font-family: Montserrat, montserrat, Source Sans, Helvetica Neue, Helvetica, Arial, sans-serif;"><font size="2"><span style="font-size:11pt">To Whom It May Concern,<br> We would like to advertise the opportunity to apply for a PhD grant in
Physics at the University of Perugia, focused on a biophysical topic.
Each year, the University of Perugia awards a PhD grant in Physics to
students who have obtained their master's degree
outside of Italy. The selection procedure involves an evaluation of the
candidates' qualifications and an interview.<br>
One of the proposed research topics for selected candidates is "Thermal
stabilization of bacterial proteome dynamics by osmolytes." Please see
the description below. The supervisors for this project will be Prof. A.
Paciaroni (University of Perugia), Judith
Peters (University Grenoble-Alpes), and Dr. F. Sterpone (CNRS LBT/IBPC
Paris).<br>
For further details, please send an email to: <a href="mailto:alessandro.paciaroni@unipg.it">alessandro.paciaroni@unipg.it</a><br>
Best regards,<br><br>
ABSTRACT: Temperature changes have profound and manifold effects on
cells. Just to give a few examples, modelling the influence of climate
change on microbial organism growth, establishing theoretical
limitations for life in severe conditions, and optimizing
thermal-based cancer treatments all require a thorough knowledge of
cell thermal stability. However, the molecular mechanisms that determine
a cell's heat sensitivity are largely unknown.<br>
Proteins are the more common and less stable macromolecules in cells;
therefore, their heat sensitivity must play a vital role as a
determinant for the majority of temperature-dependent whole-organism
actions. Very recently, we provided an unprecedented picture
of the intimate link between the proteome nanosecond time-scale
dynamics and its thermal stability, and ultimately the growth rate till
the cell?s death (Di Bari et al. ACS Cent. Sci. 2023; Caviglia et al. J.
Phys. Chem. Lett. 2024).<br>
Cells under stress conditions regulate their osmotic pressure by
accumulating small uncharged organic compounds called osmolytes.
Research conducted on monomeric, purified proteins in vitro has
demonstrated that osmolytes help maintain the stability of proteins
when exposed to high temperatures, although there is disagreement about
the exact mechanisms behind this stabilization, even more so on the
effect of osmolytes on the protein dynamics in a crowded environment.<br>
Here we propose a PhD research project to uncover the relationship
between the dynamics of the bacterial proteome and the presence of
different kinds of osmolytes as the temperature is used as a stressor
and the cell progresses toward the thermal death. This
kind of study will employ both advanced experimental techniques (such
as neutron scattering and synchrotron light scattering) and state of the
art molecular dynamics methods.<br><br><br><br><br>
Alessandro Paciaroni<br><br>
Associate Professor, Coordinator of the PhD Programme in Physics<br><br>
Head of the Laboratory of Physics of DNA and Biomolecules,<br><br>
Physics and Geology Department, University of Perugia<br><br>
Via Pascoli<br><br>
06123 Perugia Italy<br></span></font><br></div><div data-bm-signature="default"></div><style></style></div>