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Thermal response of a protein (CoVE) conformation is studied by acoarse-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-universalthermal response: Rg decays on heating in native phase (low-temperature regime)in contrast to a continuous increase on further raising the temperature beforeits saturation to a random-coil in denature phase. The globularity index (ameasure of effective dimension) of the protein decreases as the proteindenatures from a globular to a random-coil conformation.

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