# metadata.dc.description[].value
Treballs Finals de Grau de Física, Facultat de Física, Universitat de Barcelona, Curs: 2016, Tutor: Giancarlo Franzese

# metadata.dc.description.abstract[].value
Water is thought to play a crucial role in the process of cold and pressure denaturation of proteins as it has been experimentally confirmed that an important driving force behind the folding process is the minimisation of the protein’s hydrophobic surface. Water-protein interactions are therefore a vital ingredient for the understanding of such phenomena. In this report, extending previous results calculated in 2 dimensions, we use Monte Carlo simulations of a 3 dimensions coarse-grain protein model in explicit bulk water to show that the changes of water properties at the interface between the solvent and hydrophobic self-avoiding homopolymer e↵ectively lead to a stability region in the temperature-pressure plane in which the protein is folded. We find that the model is able to reproduce and rationalize the protein folding and the protein pressure denaturation at high and low pressures