OPUS-Dom: applying the folding-based method VECFOLD to determine protein domain boundaries.

ABSTRACT: In this article, we present a de novo method for predicting protein domain boundaries, called OPUS-Dom. The core of the method is a novel coarse-grained folding method, VECFOLD, which constructs low-resolution structural models from a target sequence by folding a chain of vectors representing the predicted secondary-structure elements. OPUS-Dom generates a large ensemble of folded structure decoys by VECFOLD and labels the domain boundaries of each decoy by a domain parsing algorithm. Consensus domain boundaries are then derived from the statistical distribution of the putative boundaries and three empirical sequence-based domain profiles. OPUS-Dom generally outperformed several state-of-the-art domain prediction algorithms over various benchmark protein sets. Even though each VECFOLD-gene

SUBMITTER: Wu Y 

PROVIDER: S-EPMC2753268 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature