Pinning a protein (AQP1) structure by the interacting matrix elements

The effect of temperature on a protein (AQP1) structure by a coarse-grained Monte Carlo simulation shows negative and positive responses in its native and denatured phases respectively. The same protein chain is then immersed in an interactive matrix with constitutive elements (i.e. effective solute particles with size comparable to residue) where an aquatic interactions between the residue and solute can be varied. Local and global physical quantities such as contact map, gyration radius, and structure factor are examined as a function of matrix interaction strength at a range of temperatures. The protein structures, from our preliminary studies, are found to be pinned by the solute, the radius of gyration becomes less sensitive to temperature, and structure factor shows a ramified structure with lower effective dimension than that without solute particles. In-depth analysis will be presented as the data will become available.