  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.
