Viral self-assembly as a thermodynamic process.
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.
Bruinsma
Robijn F
RF
Department of Physics and Astronomy, The University of California at Los Angeles, Los Angeles, California 90095-1569, USA.
Gelbart
William M
WM
Reguera
David
D
Rudnick
Joseph
J
Zandi
Roya
R
D002213:Capsid / Q000737:chemistry* / Q000378:metabolism; D008954:Models, Biological; D013816:Thermodynamics; D014758:Viral Core Proteins / Q000737:chemistry* / Q000378:metabolism
D014758:Viral Core Proteins