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Viral self-assembly as a thermodynamic process

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dc.creator Bruinsma, Robijn F.
dc.creator Gelbart, William M.
dc.creator Reguera, D. (David)
dc.creator Rudnick, Joseph
dc.creator Zandi, Roya
dc.date 2010-07-05T09:38:46Z
dc.date 2010-07-05T09:38:46Z
dc.date 2003
dc.date.accessioned 2024-12-16T10:24:21Z
dc.date.available 2024-12-16T10:24:21Z
dc.identifier 0031-9007
dc.identifier http://hdl.handle.net/2445/13275
dc.identifier 517565
dc.identifier.uri http://fima-docencia.ub.edu:8080/xmlui/handle/123456789/17515
dc.description 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
dc.format 4 p.
dc.format application/pdf
dc.language eng
dc.publisher American Physical Society
dc.relation Reproducció digital del document proporcionada per PROLA i http://dx.doi.org/10.1103/PhysRevLett.90.248101
dc.relation Physical Review Letters, 2003, vol. 90, núm. 24, p. 248101-1-248101-4
dc.relation http://dx.doi.org/10.1103/PhysRevLett.90.248101
dc.rights (c) American Physical Society, 2003
dc.rights info:eu-repo/semantics/openAccess
dc.source Articles publicats en revistes (Física de la Matèria Condensada)
dc.subject Biofísica
dc.subject Ciència dels materials
dc.subject Termodinàmica estadística
dc.subject Biological and medical physics
dc.subject Materials science
dc.subject Statistical thermodynamics
dc.title Viral self-assembly as a thermodynamic process
dc.type info:eu-repo/semantics/article
dc.type info:eu-repo/semantics/publishedVersion


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