Abstract
Self-organizing structures of CoVE proteins have been investigated using a coarse-grained model in Monte Carlo simulations as a function of temperature (T) in a range covering the native (low T) to denatured (high T) phases. The presence of even a few chains accelerates the very slow dynamics of an otherwise free protein chain in the native phase. The radius of gyration depends nonmonotonically on temperature and increases with the protein concentration in both the native and denatured phase. The density of organized morphology over residue-to-sample length scales (λ) is quantified by an effective dimension (D) that varies between ~ 2 at high to ~ 3 at low temperatures at λ ~ Rg with an overall lower density (D ~ 2) on larger scales. The magnitude of D depends on temperature, length scale, and concentration of proteins, i.e., D ~ 3.2 at λ ~ Rg, D ~ 2.6 at λ > Rg, and D ~ 2.0 at λ ≫ Rg, at T = 0.024.
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