Conformational response of a membrane protein (CorA) by a coarse-grained model

Conformational response of a membrane protein (CorA) plays an important role in modulating the pathways for selective transport of Mg²⁺ through its ion channel. Using a coarse-grained Monte Carlo simulation, we investigate the conformation of inner (iCorA) and outer (oCorA) segments of the protein CorA in its native and denature phases. In denature phase, the radius of gyration of both segments is found to increase with the temperature, a continuous response of iCorA and an abrupt response of oCorA [1] in a narrow range of temperature. The radius of gyration of iCorA contracts on raising the temperature in native phase in contrast while oCorA appears less organized. The conformations of these segments are quantified by estimating its effective dimension from a scaling analysis of the structure factor.
[1] S. Kitjaruwankul et al., J. Chem. Phys. 145, 135101 (2016).