Aggregation of TRP-cage by Molecular Dynamics

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

Cordoba

Congreso; SABI; 2017

Sociedad Argentina de Bioingenieria

The 20 residue long Trp-cage small protein is an excellent model for both computational 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 dynamicstructure, a stable dimmer, that preserves its core hydrophobic regions, like a micelle. It means that hydrophobic effect gives to the dimmer structure a stability being it the driving force of the aggregationprocess.