Study on collapse and folding transitions of a lattice protein using exact enumeration

Abstract

We study the conformational transitions of proteins by using the hydrophobic-polar (HP) model on a square lattice. In contrast with previous studies that relied on sampling techniques, we conducted an exhaustive enumeration of all possible conformations to obtain the density of states so that exact physical quantities could be computed. We study the conformational transitions of three sequences with varying lengths and observe both the collapse and folding transitions. The transitions exhibit distinct characteristics that depend on the sequence.