Rosetta in CASP4: Progress in ab initio protein structure prediction

Richard Bonneau, Jerry Tsai, Ingo Ruczinski, Dylan Chivian, Carol Rohl, Charlie E M Strauss, David Baker

Research output: Contribution to journalArticle

Abstract

Rosetta ab initio protein structure predictions in CASP4 were considerably more consistent and more accurate than previous ab initio structure predictions. Large segments were correctly predicted (>50 residues superimposed within an RMSD of 6.5 Å) for 16 of the 21 domains under 300 residues for which models were submitted. Models with the global fold largely correct were produced for several targets with new folds, and for several difficult fold recognition targets, the Rosetta models were more accurate than those produced with traditional fold recognition models. These promising results suggest that Rosetta may soon be able to contribute to the interpretation of genome sequence information.

Original languageEnglish (US)
Pages (from-to)119-126
Number of pages8
JournalProteins: Structure, Function and Genetics
Volume45
Issue numberSUPPL. 5
DOIs
StatePublished - Dec 1 2001

Keywords

  • CASP
  • Clustering
  • Contact order
  • Fold complexity
  • Rosetta
  • Structure prediction
  • Topology

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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  • Cite this

    Bonneau, R., Tsai, J., Ruczinski, I., Chivian, D., Rohl, C., Strauss, C. E. M., & Baker, D. (2001). Rosetta in CASP4: Progress in ab initio protein structure prediction. Proteins: Structure, Function and Genetics, 45(SUPPL. 5), 119-126. https://doi.org/10.1002/prot.1170