Viruses avoid exposure of the viral genome to harmful agents with the help of a protective protein shell known as the capsid. A secondary effect of this protective barrier is that macromolecules that may be in high concentration on the outside cannot freely diffuse across it. Therefore, inside the cell and possibly even outside, the intact virus is generally under a state of osmotic stress. Viruses deal with this type of stress in various ways. In some cases, they might harness it for infection. However, the magnitude and influence of osmotic stress on virus physical properties remains virtually unexplored for single-stranded RNA virusesthe most abundant class of viruses. Here, we report on how a model system for the positive-sense RNA icosahedral viruses, brome mosaic virus (BMV), responds to osmotic pressure. Specifically, we study the mechanical properties and structural stability of BMV under controlled molecular crowding conditions. We show that BMV is mechanically reinforced under a small external osmotic pressure but starts to yield after a threshold pressure is reached. We explain this mechanochemical behavior as an effect of the molecular crowding on the entropy of the "breathing" fluctuation modes of the virus shell. The experimental results are consistent with the viral RNA imposing a small negative internal osmotic pressure that prestresses the capsid. Our findings add a new line of inquiry to be considered when addressing the mechanisms of viral disassembly inside the crowded environment of the cell.
In this work, the HP model and Monte Carlo Method are used to study the effect hydrophobic on the folding problem. We used a lattice model and several chains with distinct proportions of hydrophobic residues. We investigate how the hydrophobic residues number of the chains can influence its folding. For each simulation, we measure three parameters: Energy, End-to-End Distance and Radius of Gyration. The geometry of the final chains was analyzed too. The simulations show that the proportion of hydrophobic residues in the chain is very important for the folding. New simulations have been showed that the position of theses residues is important to the chain.
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