Thermal denaturation of a coronavirus envelope (CoVE) protein by a coarse-grained Monte Carlo simulation

Abstract

Thermal response of an envelope protein conformation from coronavirus-2 (CoVE) is studied by a coarse-grained Monte Carlo simulation. Three distinct segments, the N-terminal, Trans-membrane, and C-terminal are verified from its specific contact profile. The radius of gyration (Rg) reveals a non-monotonic sub-universal thermal response: Rg decays substantially on heating in native phase under low-temperature regime in contrast to a continuous increase on further raising the temperature prior to its saturation to a random-coil in denature phase. The globularity index which is a measure of effective dimension of the protein, decreases as the protein denatures from a globular to a random-coil conformation.