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BP: Fachverband Biologische Physik
BP 10: Computational Biophysics II
BP 10.1: Talk
Tuesday, March 19, 2024, 09:30–09:45, H 0112
Picosecond to Microsecond Dynamics of Aggregates of an Intrinsically Disordered Protein — •Saikat Chakraborty1, Tatiana I. Morozova2, and Jean-Louis Barrat1,2 — 1Université Grenoble Alpes, CNRS, LIPhy, 38000 Grenoble, France. — 2Institut Laue-Langevin, 71 Avenue des Martyrs, 38042 Grenoble, France.
Aggregates of intrinsically disordered proteins (IDPs) can exhibit multiple time scales of fluctuations because of the widely different relaxation times of their components. Neutron backscattering or neutron spin-echo spectra of such systems carry useful dynamic information on self- and pair-correlations at several spatio-temporal regimes. However, The motions of the different segments can be correlated and time scales can be entangled. Therefore, we employ explicit solvent molecular dynamics (MD) simulations with explicit solvent to disentangle the time scales at atomistic resolution with β-casein as the IDP. Microseconds-long simulations starting from different initial configurations of the protein retain the effect of conformational diversity on the dynamics. A Systematic study of the fluctuations of different parts of the aggregates reveals that the protein side chains show Rouse-like internal dynamics at the scale of picoseconds. Whereas, the motion of the proteins is primarily that of its center of mass. At the longest time regime diffusion of center of mass of the aggregate dominates.
Keywords: Intrinsically disordered protein; Polymer; Molecular dynamics simulations; Assembly; Neutron scattering