Paolo De Los Rios

Paolo De Los Rios earned his master in Electronic Engineering at the Turin Institute of Technology (Politecnico di Torino) in May 1993. In November 1993 he moved to Trieste, Italy, to enter the PhD program in Theoretical Condensed Matter Theory at the International School for Advanced Studies (SISSA/ISAS) where he obtained the PhD degree in October 1996 for his work on the statistical physics of disordered systems. After a one year postdoc at the Max-Planck Institute for the Physics of Complex Systems in Dresden, Germany, in November 1997 he moved to the University of Fribourg, Switzerland, to join the group of Prof. Yi-Cheng Zhang. There he has worked on various applications of statistical physics to complex systems. In September 2000 he has been appointed Assistant Professor in Statistical Physics of Living Matter and Complex Systems at the Institute of Theoretical Physics of the University of Lausanne, Switzerland. Since April 2010 he is Associate Professor at the Institute of Theoretical Physics of the Ecole Polytechnique Fédérale de Lausanne (EPFL), Switzerland.

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BIOENG-606: EDCB seminar series

The EDCB seminar series provides EDCB students the opportunity to share their research and learn from their peers. Students can freely exchange, present data, ideas and get useful feedback on ongoing research and improve communication skills.

PHYS-202: Analytical mechanics (for SPH)

Présentation des méthodes de la mécanique analytique (équations de Lagrange et de Hamilton) et introduction aux notions de modes normaux et de stabilité.

PHYS-441: Statistical physics of biomacromolecules

Introduction to the application of the notions and methods of theoretical physics to problems in biology.

Protein

Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing met

Protein folding

Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologicall

Polymer

A polymer (ˈpɒlᵻmər; Greek poly-, "many" + -mer, "part") is a substance or material consisting of very large molecules called macromolecules, composed of many repeating subunits. Due to their broad

Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8-9, 2022

Paolo De Los Rios, Pierre Goloubinoff, Wei Li

The Second International Symposium on Cellular and Organismal Stress Responses took place virtually on September 8-9, 2022. This meeting was supported by the Cell Stress Society International (CSSI) and organized by Patricija Van OostenHawle and Andrew Truman (University of North Carolina at Charlotte, USA) and Mehdi Mollapour (SUNY Upstate Medical University, USA). The goal of this symposium was to continue the theme from the initial meeting in 2020 by providing a platform for established researchers, new investigators, postdoctoral fellows, and students to present and exchange ideas on various topics on cellular stress and chaperones. We will summarize the highlights of the meeting here and recognize those that received recognition from the CSSI.

SPRINGER2023

A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70

Salvatore Assenza, Paolo De Los Rios, Bruno Claude Daniel Fauvet, Pierre Goloubinoff

Detailed understanding of the mechanism by which Hsp70 chaperones protect cells against protein aggregation is hampered by the lack of a comprehensive characterization of the aggregates, which are typically heterogeneous. Here we designed a reporter chaperone substrate, MLucV, composed of a stress-labile luciferase flanked by stress-resistant fluorescent domains, which upon denaturation formed a discrete population of small aggregates. Combining Forster resonance energy transfer and enzymatic activity measurements provided unprecedented details on the aggregated, unfolded, Hsp70-bound and native MLucV conformations. The Hsp70 mechanism first involved ATP-fueled disaggregation and unfolding of the stable pre-aggregated substrate, which stretched MLucV beyond simply unfolded conformations, followed by native refolding. The ATP-fueled unfolding and refolding action of Hsp70 on MLucV aggregates could accumulate native MLucV species under elevated denaturing temperatures highly adverse to the native state. These results unambiguously exclude binding and preventing of aggregation from the non-equilibrium mechanism by which Hsp70 converts stable aggregates into metastable native proteins.

NATURE PORTFOLIO2022

Emergent thermophoretic behavior in chemical reaction systems

Daniel Maria Busiello, Paolo De Los Rios, Shiling Liang

Exposing a solution to a temperature gradient can lead to the accumulation of particles on either the cold or warm side. This phenomenon is known as thermophoresis, and its microscopic origin is still debated. Here, we show that thermophoresis can be observed in any system having internal states with different transport properties, and temperature-modulated rates of transitions between the states. These internal degrees of freedom might be configurational, chemical or velocity states. We also derive an expression for the Soret coefficient, which decides whether particles accumulate on the cold or warm side. Our framework can be applied to any chemical reaction system diffusing in a temperature gradient. It also captures the possibility to observe a sign inversion of the Soret coefficient as the competition between chemical and velocity states. We establish thermophoresis as a genuine non-equilibrium effect, originating from internal microscopic currents consistent with the necessity of transporting heat from warm to cold regions.

IOP Publishing Ltd2022