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Structure prediction of partial-length protein sequences

  • University of Washington

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Protein structure information is essential to understand protein function. Computational methods to accurately predict protein structure from the sequence have primarily been evaluated on protein sequences representing full-length native proteins. Here, we demonstrate that top-performing structure prediction methods can accurately predict the partial structures of proteins encoded by sequences that contain approximately 50% or more of the full-length protein sequence. We hypothesize that structure prediction may be useful for predicting functions of proteins whose corresponding genes are mapped expressed sequence tags (ESTs) that encode partial-length amino acid sequences. Additionally, we identify a confidence score representing the quality of a predicted structure as a useful means of predicting the likelihood that an arbitrary polypeptide sequence represents a portion of a foldable protein sequence (foldability). This work has ramifications for the prediction of protein structure with limited or noisy sequence information, as well as genome annotation.

Original languageEnglish
Pages (from-to)14892-14907
Number of pages16
JournalInternational Journal of Molecular Sciences
Volume14
Issue number7
DOIs
StatePublished - Jul 2013

Keywords

  • EST
  • Expressed sequence tag
  • Protein design
  • Protein folding
  • Protein structure prediction

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