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Computational design of water-soluble α-helical barrels

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)485-488
Number of pages4
JournalScience
Volume346
Issue number6208
DOIs
DateAccepted/In press - 19 Sep 2014
DatePublished (current) - 24 Oct 2014

Abstract

The design of protein sequences that fold into prescribed de novo structures is challenging. General solutions to this problem require geometric descriptions of protein folds and methods to fit sequences to these. The α-helical coiled coils present a promising class of protein for this and offer considerable scope for exploring hitherto unseen structures. For α-helical barrels, which have more than four helices and accessible central channels, many of the possible structures remain unobserved. Here, we combine geometrical considerations, knowledge-based scoring, and atomistic modeling to facilitate the design of new channel-containing α-helical barrels. X-ray crystal structures of the resulting designs match predicted in silico models. Furthermore, the observed channels are chemically defined and have diameters related to oligomer state, which present routes to design protein function.

    Structured keywords

  • BrisSynBio
  • Bristol BioDesign Institute

    Research areas

  • Oligomer, water, peptide, protein

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