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ABSTRACT: Background
Reduced representations of proteins have been playing a keyrole in the study of protein folding. Many such models are available, with different representation detail. Although the usefulness of many such models for structural bioinformatics applications has been demonstrated in recent years, there are few intermediate resolution models endowed with an energy model capable, for instance, of detecting native or native-like structures among decoy sets. The aim of the present work is to provide a discrete empirical potential for a reduced protein model termed here PC2CA, because it employs a PseudoCovalent structure with only 2 Centers of interactions per Amino acid, suitable for protein model quality assessment.Results
All protein structures in the set top500H have
SUBMITTER: Fogolari F
PROVIDER: S-EPMC1854906 | biostudies-literature | 2007 Mar
REPOSITORIES: biostudies-literature