Thermal-induced folding and unfolding of a transmembrane protein (CorA)

Thermal response of the inner (iCorA) and outer (oCorA) segments of a transmembrane protein CorA is investigated by a large-scale coarse-grained Monte Carlo simulation in native phase. We find that the conformation of iCorA contracts on raising the temperature, in contrast to its thermal response in denatured phase. The conformational response of the oCorA in its native phase appears to be less organized but differs considerably from that in its denatured phase where an abrupt increase of its radius of gyration occurs in a narrow temperature range. The inner segment (iCorA) retains its globular conformation in native phase while oCorA resorts to random-coil configurations with some coagulations on raising the temperature.