Finding low-energy conformations of lattice protein models by quantum annealing.

ABSTRACT: Lattice protein folding models are a cornerstone of computational biophysics. Although these models are a coarse grained representation, they provide useful insight into the energy landscape of natural proteins. Finding low-energy threedimensional structures is an intractable problem even in the simplest model, the Hydrophobic-Polar (HP) model. Description of protein-like properties are more accurately described by generalized models, such as the one proposed by Miyazawa and Jernigan (MJ), which explicitly take into account the unique interactions among all 20 amino acids. There is theoretical and experimental evidence of the advantage of solving classical optimization problems using quantum annealing over its classical analogue (simulated annealing). In this report, we present a benchmark

SUBMITTER: Perdomo-Ortiz A 

PROVIDER: S-EPMC3417777 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature