138 research outputs found
Beyond icosahedral symmetry in packings of proteins in spherical shells
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) that optimizing those flexibilities can be a
possible design strategy to obtain regular synthetic cages with full control
over their surface properties.Comment: 8 pages, 5 figure
How do miniproteins fold?
A high-throughput study yields libraries of miniproteins that help to explain how proteins are stabilized</jats:p
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