Session A9 - Proteins.
ORAL session, Monday morning, March 22
510B, Palais des Congres
Proteins folding problem is an important topic in both experimental and theoretical studies. Conventional, reaction kinetics of protein folding is determined by specific structure forming. However the global stability of protein may not directly relate to partial structure formation. In this study, we directly investigated protein folding stability and its mechanism by both experimental approach and molecular simulation. During the experiment unfolded protein was drop directly into native solution environment. Both aggregated and soluble protein can be obtained. Meanwhile a molecular simulation study indicated that proteins followed random walk process and then aggregated when they collided to each other. However, proteins did not aggregate when they reached to stable state. This indicated that protein folding is an antagonistic reaction between diffusion-limited aggregation (DLA) and spontaneously folding. By changing the mean-free path of unfolded protein, the fraction of aggregated protein decay followed the function of logistic function, a limited growth model. The correlation time of protein aggregation indicated that the proteins is stable as fast as 22 microsecond.