Aggregation of TRP-cage by Molecular Dynamics

MEYRA ARIEL GERMAN; FAUNDEZ CRISTIAN; C. GASTÓN FERRARA; YANIS RICARDO ESPINOSA SILVA

Congreso; XXI Congreso Argentino de Bioingeniería y X Jornadas de Ingeniería Clínica; 2017

The 20 residue long Trp-cage small protein is an excellent model for bothcomputational and experimental studies of protein folding, stability, and aggregation. In this simulation at NVT ensemble, it is studied the aggregation process of a solution of folded protein. Our results show a highly dynamic structure, a stable dimmer, that preserves its corehydrophobic regions, like a micelle. It means that hydrophobic effect gives to the dimmer structure a stability being it the driving force of the aggregation process.