The folding of a protein to its native state is critical for the correct functioning of the cell. When proteins do not fold correctly, they can self-assembly into large aggregate structures that can deposit on organs in the body. A number of diseases, including Type II Diabetes and Alzheimer’s Disease, are associated with this pathological process. Under cellular conditions, proteins encounter a variety of surfaces, from chaperones to membranes, that can dramatically alter folding and assembly pathways. In this talk, I will present atomistic and coarse-grained simulations that probe the effect of surfaces on protein folding and aggregation mechanisms.
Refreshments in CW 119 at 4:15 p.m.