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

Pinning the conformation of a protein (CorA) in a solute matrix with selective binding

“…It is worth pointing out that we have already examined the structure and dynamics of CorA in absence of environmental complexity and found interesting thermal response of inner and outer segments of the protein [10,11]. For example, the thermal response of the inner segment shows a continuous transition from globular to random-coil structure on raising the temperature while the outer segment exhibits an abrupt (nearly discontinuous) thermal response in a narrow range of temperature.…”

“…A bond-fluctuation mechanism [13] is used to model the protein [10][11][12], a chain of 351 nodes, each representing unique specificity of corresponding residue. The simulation is performed on a cubic lattice with ample degrees of freedom for each residue to perform its stochastic moves and corresponding peptide bonds to fluctuate.…”

“…The interplay between the solute-residue interaction and thermal agitation may lead to unique structural evolution. This article is focused on the effect of the strength of interaction on the selective binding of residues with the mobile solute particles and the structural evolution of CorA at a low (native phase) and a high (denatured phase) temperature [11].…”

“…For example, the thermal response of the inner segment shows a continuous transition from globular to random-coil structure on raising the temperature while the outer segment exhibits an abrupt (nearly discontinuous) thermal response in a narrow range of temperature. Unlike in denatured phase, the conformation of the inner segment contracts on raising the temperature in its native phase where the outer segment appears less organized [11]. In an implicit effective medium, the size of the inner segment of the protein decreases in native phase and increases in denatured phase before reaching saturation with the residue-matrix interaction strength; the outer segment shows opposite response to effective medium [12].…”