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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/13275

Viral self-assembly as a thermodynamic process

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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

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BRUINSMA, Robijn F., et al. Viral self-assembly as a thermodynamic process. Physical Review Letters. 2003. Vol. 90, num. 24, pags. 248101-1-248101-4. ISSN 0031-9007. [consulted: 14 of August of 2026]. Available at: https://hdl.handle.net/2445/13275

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