Ref HAL: hal-01360415_v1
Ref Arxiv: 1604.05532
DOI: 10.1063/1.4959034
WoS: 000381679800009
Ref. & Cit.: NASA ADS
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7 Citations
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We employ a field-theoretical variational approach to study the behavior of ionic solutions in the grand canonical ensemble. To describe properly the hardcore interactions between ions, we use a cutoff in Fourier space for the electrostatic contribution of the grand potential and the Carnahan-Starling equation of state with a modified chemical potential for the pressure one. We first calibrate our method by comparing its predictions at room temperature with Monte Carlo results for excess chemical potential and energy. We then validate our approach in the bulk phase by describing the classical “ionic liquid-vapor” phase transition induced by ionic correlations at low temperature, before applying it to electrolytes at room temperature confined to nanopores embedded in a low dielectric medium and coupled to an external reservoir of ions. The ionic concentration in the nanopore is then correctly described from very low bulk concentrations, where dielectric exclusion shifts the transition up to room temperature for sufficiently tight nanopores, to high concentrations where hardcore interactions dominate which, as expected, modify only slightly this ionic “capillary evaporation.”

Ref HAL: hal-01360270_v1
Ref Arxiv: 1602.07524
DOI: 10.1103/PhysRevLett.116.176801
WoS: WOS:000374964400010
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39 Citations
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By numerical simulations and analytical studies, we show that the phenomenon of microwave-induced resistance oscillations can be understood as a classical memory effect caused by re-collisions of electrons with scattering centers after a cyclotron period. We develop a Drude-like approach to magneto-transport in presence of a microwave field, taking account of memory effects, and find an excellent agreement between numerical and analytical results, as well as a qualitative agreement with experiment.

Commentaires: 6 pages, 3 figures. Réf Journal: Phys. Rev. Lett. 116, 176801 (2016)

Ref HAL: hal-01345990_v1
DOI: 10.1038/srep27215
WoS: WOS:000377338000001
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Cyclin A2 is a key player in the regulation of the cell cycle. Its degradation in mid-mitosis depends primarily on the ubiquitin-proteasome system (UPS), while autophagy also contributes. However, a fraction of cyclin A2 persists beyond metaphase. In this work, we focus on cyclin A2-rich foci detected in mitosis by high resolution imaging and analyse their movements. We demonstrate that cyclin A2 interacts with actin and RhoA during mitosis, and that cyclin A2 depletion induces a dramatic decrease in active RhoA in mitosis. Our data suggest cyclin A2 participation in RhoA activation in late mitosis.

Ref HAL: hal-01319073_v1
PMID 27300929
DOI: 10.1103/PhysRevE.93.052412
WoS: 000376262700007
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4 Citations
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We consider the symmetry and physical origin of collective displacement modes playing a crucial role in the morphological transformation during the maturation of the HK97 bacteriophage and similar viruses. It is shown that the experimentally observed hexamer deformation and pentamer twist in the HK97 procapsid correspond to the simplest irreducible shear strain mode of a spherical shell. We also show that the icosahedral faceting of the bacteriophage capsid shell is driven by the simplest irreducible radial displacement field. The shear field has the rotational icosahedral symmetry group I while the radial field has the full icosahedral symmetry I_{h}. This difference makes their actions independent. The radial field sign discriminates between the icosahedral and the dodecahedral shapes of the faceted capsid shell, thus making the approach relevant not only for the HK97-like viruses but also for the parvovirus family. In the frame of the Landau-Ginzburg formalism we propose a simple phenomenological model valid for the first reversible step of the HK97 maturation process. The calculated phase diagram illustrates the discontinuous character of the virus shape transformation. The characteristics of the virus shell faceting and expansion obtained in the in vitro and in vivo experiments are related to the decrease in the capsid shell thickness and to the increase of the internal capsid pressure.

Ref HAL: hal-01304303_v1
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Principles of formation of viral capsids with double protein shells

Résumé:

Physics of virus self-assembly and virus-like biological nanoparticles

Résumé:

Physics of Virus Self-Assembly