Monte Carlo Simulations of Coarse-grained Protein Models for Crambin

In order to study interactions of primary importance in protein folding, we apply Wang-Landau sampling [1] and a novel histogram-free multicanonical sampling algorithm [2] to the hydrophobic-polar (HP) [3] and H0P [4] lattice protein models, as well as their continuum versions inspired by the AB model [5]. These models offer significant computational advantage over all-atom models, due to simplified interactions and the reduction of the 20 amino acids to a limited number of types. In this work, we compare and contrast folding behavior between such models for Crambin - a 46 amino acid plant protein, and for a homopolymer of the same length. Our results highlight the strengths of the two simulational frameworks and the differences in folding between models.

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