New encouraging developments in contact prediction: Assessment of the CASP11 results

Proteins. 2016 Sep;84 Suppl 1(Suppl 1):131-44. doi: 10.1002/prot.24943. Epub 2015 Nov 17.

Abstract

This article provides a report on the state-of-the-art in the prediction of intra-molecular residue-residue contacts in proteins based on the assessment of the predictions submitted to the CASP11 experiment. The assessment emphasis is placed on the accuracy in predicting long-range contacts. Twenty-nine groups participated in contact prediction in CASP11. At least eight of them used the recently developed evolutionary coupling techniques, with the top group (CONSIP2) reaching precision of 27% on target proteins that could not be modeled by homology. This result indicates a breakthrough in the development of methods based on the correlated mutation approach. Successful prediction of contacts was shown to be practically helpful in modeling three-dimensional structures; in particular target T0806 was modeled exceedingly well with accuracy not yet seen for ab initio targets of this size (>250 residues). Proteins 2016; 84(Suppl 1):131-144. © 2015 Wiley Periodicals, Inc.

Keywords: CASP; co-variation; contact prediction; correlated mutations; evolutionary coupling.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Amino Acid Sequence
  • Bacteria / chemistry
  • Computational Biology / methods
  • Computational Biology / statistics & numerical data*
  • Computer Simulation
  • Databases, Protein
  • Escherichia coli Proteins / chemistry*
  • Humans
  • International Cooperation
  • Internet
  • Models, Molecular*
  • Models, Statistical*
  • Protein Folding
  • Protein Interaction Domains and Motifs
  • Protein Structure, Secondary
  • Proteins / chemistry*
  • Sequence Alignment
  • Software*

Substances

  • Escherichia coli Proteins
  • Proteins
  • YaaA protein, E coli