| Summary: | 碩士 === 國立東華大學 === 應用物理研究所 === 92 === Abstract:
In this study, we investigated protein folding stability and its mechanism directly by both experimental approach and molecular simulation. During the direct folding experiment, the unfolded protein was dropped into native solution environment directly. Both aggregated and soluble protein can be obtained. This indicated that both aggregation and spontaneously folding processes may take place during the folding process. Meanwhile a molecular simulation study indicated that proteins moved randomly in unfolding state and then aggregated when they collided to each other. Therefore, this process was regulated by its diffusive behavior. However, proteins did not aggregate when it reached to a stable state. Therefore, we concluded that the spontaneously folding and diffusion limited aggregation take place at the same time. Therefore we may also conclude that protein folding is an antagonist reaction between diffusion- limited aggregation (DLA) and self-assembly (spontaneously folding). By changing the mean-free path (or mean-free time or concentration) of unfolded protein, the fraction of aggregated protein decay followed the function of logistic function, a limited growth model. The critical time of its autocorrelation function indicated that the protein is stable on a submillisecond time scale, in vitro.
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