Abstract
Abstract
In this article, a protein sequence of length n is embedded in a two-dimensional lattice with m (>n) points. Thus the obtained minimal energy configurations are expected to have flexible shapes in contrast to the compact rectangular conformations. To fulfill this extension, the elastic net algorithm is modified to deal with the difficulty brought by the unsymmetrical relationship between amino acids and lattice points. New set partition strategy in the embedding phase is introduced, and two local search methods are applied to overcome the multimapping phenomena. Several HP benchmark examples with up to 48 amino acids are tested to verify the effectiveness of the proposed approach.
Get full access to this article
View all access options for this article.
