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

Abstract

Thermal response of a protein (CoVE) conformation 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) is found to exhibit a non-monotonic sub-universal thermal response: Rg decays on heating in native phase (low-temperature regime) in contrast to a continuous increase on further raising the temperature before its saturation to a random-coil in denature phase. The globularity index (a measure of effective dimension) of the protein decreases as the protein denatures from a globular to a random-coil conformation.