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Phys. Rev. Lett. 90, 248101 (2003) [4 pages]

Viral Self-Assembly as a Thermodynamic Process

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Robijn F. Bruinsma1, William M. Gelbart2, David Reguera2, Joseph Rudnick1, and Roya Zandi2
1Department of Physics and Astronomy, The University of California at Los Angeles, Los Angeles, California 90095-1569, USA
2Department of Chemistry and Biochemistry, The University of California at Los Angeles, Los Angeles, California 90095-1569, USA

Received 6 November 2002; published 17 June 2003

The protein shells, or capsids, of nearly all spherelike viruses adopt icosahedral symmetry. In the present Letter, 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.

© 2003 The American Physical Society

URL:
http://link.aps.org/doi/10.1103/PhysRevLett.90.248101
DOI:
10.1103/PhysRevLett.90.248101
PACS:
87.15.Nn, 61.50.Ah, 81.16.Dn, 87.16.Dg