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• W2077515504 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-generated structure contains large errors, collectively these structures provide a more robust delineation of domain boundaries. The success of OPUS-Dom suggests that the arrangement of protein domains is more a consequence of limited coordination patterns per domain arising from tertiary packing of secondary-structure segments, rather than sequence-specific constraints." @default.
• W2077515504 created "2016-06-24" @default.
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• W2077515504 date "2009-01-01" @default.
• W2077515504 modified "2023-10-17" @default.
• W2077515504 title "OPUS-Dom: Applying the Folding-Based Method VECFOLD to Determine Protein Domain Boundaries" @default.
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• W2077515504 doi "https://doi.org/10.1016/j.jmb.2008.10.093" @default.
• W2077515504 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2753268" @default.
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• W2077515504 hasPublicationYear "2009" @default.
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