Energy landscape and dynamics of an HP lattice model of proteins —The role of anisotropy
1 Institute of Physics, Polish Academy of Sciences - 02-668 Warsaw, Poland
2 Department of Physics, University of Maryland - College Park, MD 20742, USA
Received: 10 October 2013
Accepted: 29 November 2013
We present the results of exact numerical studies of the energy landscape and the dynamics of a 12-monomer chain comprised of two types of amino acids called the HP model. We benchmark our findings against the corresponding results of previous studies of a Go model, which encodes the native state conformation. We also show how the energy landscape gets modified dramatically and improves the folding properties on incorporating the inherent anisotropy of a chain, albeit in a simplified manner.
PACS: 87.10.-e – General theory and mathematical aspects / 87.10.Hk – Lattice models / 87.15.A- – Theory, modeling, and computer simulation
© EPLA, 2013