Simulação computacional do modelo HP generalizado para proteínas

Abstract

We consider a generalized hydrophobic-polar model for proteins on square and cubic lat- tices. Besides the attraction between nonbonded hydrophobic monomers, the present

model also takes into account an interaction between hydrophobic and polar units. By

using the pruned-enriched Rosenbluth method (PERM), we investigate a specific poly- mer sequence composed of 42 monomers that has been proposed to simulate the physical

properties of the parallel β-helix of pectate lyase C. For each temperature, the total number of generated chains varies from 106 to 107

. Physical observables such as speci- fic heat, total energy, end-to-end distance, radius of gyration, and the average number

of hydrophobic-hydrophobic and hydrophobic-polar contacts, are evaluated for different values of the parameter s, which corresponds to the ratio between the hydrophobic-polar and the hydrophobic-hydrophobic contact energies. Eventually, a pseudo-phase diagram in the space of temperature and the ratio of contact energy scales is constructed.