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Beyond icosahedral symmetry in packings of proteins in spherical shells

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)9014-9019
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume114
Issue number34
Early online date8 Aug 2017
DOIs
DateAccepted/In press - 10 Jul 2017
DateE-pub ahead of print - 8 Aug 2017
DatePublished (current) - 22 Aug 2017

Abstract

The formation of quasi-spherical cages from protein building blocks is a remarkable self-assembly process in many natural systems, where a small number of elementary building blocks are assembled to build a highly symmetric icosahedral cage. In turn, this has inspired synthetic biologists to design de novo protein cages. We use simple models, on multiple scales, to investigate the self-assembly of a spherical cage, focusing on the regularity of the packing of protein-like objects on the surface. Using building blocks, which are able to pack with icosahedral symmetry, we examine how stable these highly symmetric structures are to perturbations that may arise from the interplay between flexibility of the interacting blocks and entropic effects. We find that, in the presence of those perturbations, icosahedral packing is not the most stable arrangement for a wide range of parameters; rather disordered structures are found to be the most stable. Our results suggest that (i) many designed, or even natural, protein cages may not be regular in the presence of those perturbations and (ii) optimizing those flexibilities can be a possible design strategy to obtain regular synthetic cages with full control over their surface properties.

    Research areas

  • Coarse-grain modeling, Icosahedral symmetry, Protein cage, Self-assembly, Protein design

    Structured keywords

  • Bristol BioDesign Institute
  • QITG
  • BrisSynBio

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  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via PNAS at http://www.pnas.org/content/early/2017/08/07/1706825114.abstract. Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 2.43 MB, PDF document

  • Supplementary information PDF

    Accepted author manuscript, 3.39 MB, PDF document

DOI

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