title: Using a reduced dimensionality model to compute the thermodynamic properties of finite polypeptide aggregates.
abstract: By implementing a simple reduced dimensionality model to describe the interactions in finite systems composed of two seven-amino-acid peptides, the thermodynamic properties of ordered and disordered aggregates were computed. Within this model, the hydrophobicity of each amino acid was varied, and the stability of the systems computed. Accurate averages in the canonical ensemble were obtained using various replica exchange Monte Carlo algorithms. Low and high temperature regions were encountered where the ordered and disordered aggregates were stabilized. It was observed that as the degree of hydrophobicity increased, the stability of the aggregates increased, with a significant energetic stabilization obtained for the ordered aggregates. Upon decreasing the concentration of the solution, the stability of the amorphous aggregates increased when compared to the ordered systems.
authors.affiliation: Department of Chemistry, University of Puerto Rico, at Mayagüez, Mayagüez, P.R. 00681 USA ; Department of Chemistry, Lehman College-CUNY, Bronx, NY 10468 USA.
authors.forename: Gustavo E
authors.initials: GE
authors.lastname: López
authors.forename: Anthony
authors.initials: A
authors.lastname: Cruz
authors.forename: Melyorise
authors.initials: M
authors.lastname: Sepulveda-Chervony
authors.forename: Juan
authors.initials: J
authors.lastname: López-Garriga
authors.forename: Madeline
authors.initials: M
authors.lastname: Torres-Lugo
keywords: Finite systems; Monte Carlo; Peptides; Replica exchange