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Jun 8 – 11, 2021 Online only
Europe/Berlin timezone
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Neutron Scattering Experiments and Multi-Scale Simulations Reveal Dynamical Properties of the Bacterial Cytoplasm Near Cell-Death Temperature

Jun 10, 2021, 11:30 AM
Talk Protein structure, function and dynamics Protein structure, function and dynamics


Daniele Di Bari (University of Perugia and University Grenoble-Alpes)


Daniele Di Bari1,2,3, Stepan Timr4, Fabio Sterpone4, Alessandro Paciaroni1, Judith Peters2,3.

1Univ. of Perugia, Dep. of Physics and Geology, Italy. 2Univ. Grenoble-Alpes, CNRS, LiPhy, France. 3Institut Laue-Langevin, France. 4Laboratoire de Biochimie Theorique, CNRS, France.

Life on Earth exhibits an amazing adaptive capacity to a vast range of temperatures. While the molecular mechanisms underlying such adaptability are not yet fully understood, it has been proposed that the temperature of cellular death coincides with a catastrophic denaturation of the proteome. Here we combine incoherent quasi-elastic and elastic neutron scattering experiments with multi-scale molecular dynamics simulations to describe the dynamical features of the proteins in the E. Coli cytoplasm when approaching thermal denaturation, and to characterize distinct contributions to their pico- to nanosecond dynamics. Moreover, we test the validity of the Lindemann criterion — linking structural fluctuations and melting — in cell-like conditions.
Our results allow us to rationalize the existence of a specific dynamical regime revealed by neutron scattering experiments to be a general signature around cell-death temperature.

Primary authors

Daniele Di Bari (University of Perugia and University Grenoble-Alpes) Judith Peters (Université Grenoble Alpes) Alessandro Paciaroni (University of Perugia) Dr Fabio Sterpone (LBT CNRS) Dr Stepan Timr (LBT CNRS)

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