Viral self-assembly as a thermodynamic process

Details Viral self-assembly as a thermodynamic process Viral self-assembly as a thermodynamic process

2002-11-18

arxiv.org/abs/cond-mat/0211390v2

Phys. Rev. Lett. 90, 248101 (2003)

Physics

Condensed Matter

Soft Condensed Matter

pdf file, 13 pages, three figures

Scientific paper

10.1103/PhysRevLett.90.248101

The protein shells, or capsids, of all sphere-like viruses adopt icosahedral symmetry. In the present paper we propose a statistical thermodynamic model for viral self-assembly. We find that icosahedral symmetry is not expected for viral capsids constructed from structurally identical protein subunits and that this symmetry requires (at least) two internal "switching" configurations of the protein. Our results indicate that icosahedral symmetry is not a generic consequence of free energy minimization but requires optimization of internal structural parameters of the capsid proteins.

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