Statistical Physics of Viral Capsids with Broken Symmetry.
We present a model to understand quantitatively the role of symmetry breaking in assembly of macromolecular aggregates in general, and the protein shells of viruses in particular. A simple dodecahedral lattice model with a quadrupolar order parameter allows us to demonstrate how symmetry breaking may reduce the probability of assembly errors and, consequently, enhance assembly efficiency. We show that the ground state is characterized by large-scale cooperative zero-energy modes. In analogy with other models, this suggests a general physical principle: the tendency of biological molecules to generate symmetric structures competes with the tendency to break symmetry in order to achieve specific functional goals.
Department of Mechanical and Aerospace Engineering, University of California, Los Angeles, California 90095, USA.
L E
LE
Perotti
Department of Physics and Astronomy, University of California, Los Angeles, California 90095, USA.
J
J
Rudnick
Department of Physics and Astronomy, University of California, Los Angeles, California 90095, USA.|Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095, USA.|California NanoSystems Institute, University of California, Los Angeles, California 90095, USA.
R F
RF
Bruinsma
Department of Mechanical and Aerospace Engineering, University of California, Los Angeles, California 90095, USA.|California NanoSystems Institute, University of California, Los Angeles, California 90095, USA.
W S
WS
Klug
D036022:Capsid Proteins / Q000737:chemistry* / Q000378:metabolism*; D046911:Macromolecular Substances / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D008956:Models, Chemical; D008958:Models, Molecular; D066329:Protein Aggregates; D017906:Siphoviridae / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
D036022:Capsid Proteins; D046911:Macromolecular Substances; D066329:Protein Aggregates