stability properties
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Universe ◽  
2021 ◽  
Vol 8 (1) ◽  
pp. 6
Author(s):  
Bernardo F. de Aguiar ◽  
Raissa F. P. Mendes ◽  
Felipe T. Falciano

Screening mechanisms are often deployed by dark energy models to conceal the effects of their new degrees of freedom from the scrutiny of terrestrial and solar system experiments. However, the extreme properties of nuclear matter may lead to a partial failure of screening mechanisms inside the most massive neutron stars observed in nature, opening up the possibility of probing these theories with neutron star observations. In this work, we explore equilibrium and stability properties of neutron stars in two variants of the symmetron model. We show that around sufficiently compact neutron stars, the symmetron is amplified with respect to its background (cosmological) value by several orders of magnitude, and that the properties of such unscreened stars are sensitive to corrections to the leading linear coupling between the symmetron and matter.


2021 ◽  
Vol 1 ◽  
Author(s):  
Sankar Basu ◽  
Simon S. Assaf ◽  
Fabian Teheux ◽  
Marianne Rooman ◽  
Fabrizio Pucci

Understanding the role of stability strengths and weaknesses in proteins is a key objective for rationalizing their dynamical and functional properties such as conformational changes, catalytic activity, and protein-protein and protein-ligand interactions. We present BRANEart, a new, fast and accurate method to evaluate the per-residue contributions to the overall stability of membrane proteins. It is based on an extended set of recently introduced statistical potentials derived from membrane protein structures, which better describe the stability properties of this class of proteins than standard potentials derived from globular proteins. We defined a per-residue membrane propensity index from combinations of these potentials, which can be used to identify residues which strongly contribute to the stability of the transmembrane region or which would, on the contrary, be more stable in extramembrane regions, or vice versa. Large-scale application to membrane and globular proteins sets and application to tests cases show excellent agreement with experimental data. BRANEart thus appears as a useful instrument to analyze in detail the overall stability properties of a target membrane protein, to position it relative to the lipid bilayer, and to rationally modify its biophysical characteristics and function. BRANEart can be freely accessed from http://babylone.3bio.ulb.ac.be/BRANEart.


Author(s):  
Erin Carson ◽  
Kathryn Lund ◽  
Miroslav Rozložník ◽  
Stephen Thomas
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2021 ◽  
Vol 79 ◽  
pp. 101805
Author(s):  
Lynn Heller ◽  
Sebastian Heller ◽  
Cheikh Birahim Ndiaye
Keyword(s):  

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