Ref HAL: hal-01109708_v2
DOI: 10.1134/S1063783415040125
WoS: 000352906700025
Exporter : BibTex | endNote
3 Citations
Résumé:

Spherical viral shells with icosahedral symmetry are considered as quasicrystalline tilings. Similarly to known Caspar-Klug quasi-equivalence theory, the presented approach also minimizes the number of conformations necessary for the protein molecule bonding with its neighbors in the shell, but is based on different geometrical principles. It is assumed that protein molecule centers are located at vertices of tiles with identical edges, and the number of different tile types is minimal. Idealized coordinates of nonequivalent by symmetry protein positions in six various capsid types are obtained. The approach describes in a uniform way both the structures satisfying the well-known Caspar and Klug geometrical model and the structures contradicting this model.