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The self-organizing dynamics of lysozymes (an amyloid protein with 148 residues) with different numbers of protein chains, = , and (concentration ) is studied by a coarse-grained Monte Carlo simulation with knowledge-based residue-residue interactions. The dynamics of an isolated lysozyme ( = ) is ultra-slow (quasi-static) at low temperatures and becomes diffusive asymptotically on raising the temperature. In contrast, the presence of interacting proteins leads to concentration induced protein diffusion at low temperatures and concentration-tempering sub-diffusion at high temperatures. Variation of the radius of gyration of the protein with temperature shows a systematic transition from a globular structure (at low ) to a random coil (high ) conformation when the proteins are isolated. The crossover from globular to random coil becomes sharper upon increasing the protein concentration (i.e. with = ), with larger at higher temperatures and concentration; becomes smaller on adding more protein chains (e.g. = ) a non-monotonic response to protein concentration. Analysis of the structure factor (()) provides an estimate of the effective dimension (, globular conformation at low temperature, and , random coil, at high temperatures) of the isolated protein. With many interacting proteins, the morphology of the self-assembly varies with scale, i.e. at the low temperature ( = ), on the scale comparable to the radius of gyration of the protein, and at the large scale over the entire sample. The global network of fibrils appears at high temperature ( = ) with (i.e. a random coil morphology at large scale) involving tenuous distribution of micro-globules (at small scales).


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