Electrostatic interactions and structural transformations in viral shells.

Structural transformations occurring in proteinaceous viral shells (capsids) can be induced by changing the pH of bathing solution, thus modifying the dissociation equilibrium of ionizable amino acids in proteins. To analyze the effects of electrostatic interactions on viral capsids, we construct a model of 2D isotropic elastic shells with embedded point charges located in the centers of mass of individual proteins. We find that modification of the electrostatic interactions between proteins affects not only the size and shape of capsids, but in addition induces substantial deformations of hexamers in capsid structures.

Topological balance of cell distributions in plane monolayers.

Most of normal proliferative epithelia of plants and metazoans are topologically invariant and characterized by similar cell distributions according to the number of cell neighbors (DCNs). Here we study peculiarities of these distributions and explain why the DCN obtained from the location of intercellular boundaries and that based on the Voronoi tessellation with nodes located on cell nuclei may differ from each other. As we demonstrate, special microdomains where four or more intercellular boundaries converge are topologically charged.

Theory of density waves and organization of proteins in icosahedral virus capsids.

Understanding the physical principles underlying the structural organization of the proteinaceous viral shells is of major importance to advance antiviral strategies. Here, we develop a phenomenological thermodynamic theory, which considers structures of small and middle-size icosahedral viral shells as a result of condensation of a minimum number of protein density waves on a spherical surface. Each of these irreducible critical waves has icosahedral symmetry and can be expressed as a specific series of the spherical harmonics with the same wave number .

Close packings of identical proteins in small spherical capsids and similar proteinaceous shells.

Understanding the principles governing protein arrangement in viral capsids and structurally similar protein shells can enable the development of new antiviral strategies and the design of artificial protein cages for various applications. We study these principles within the context of the close packing problem, by analyzing dozens of small spherical shells assembled from a single type of protein. First, we use icosahedral spherical close packings containing 60 identical disks, where ≤ 4, to rationalize the protein arrangement in twenty real icosahedral shells both satisfying and violating the paradigmatic Caspar-Klug model.

Topological properties and shape of proliferative and nonproliferative cell monolayers.

During embryonic development, structures with complex geometry can emerge from planar epithelial monolayers; studying these shape transitions is of key importance for revealing the biophysical laws involved in the morphogenesis of biological systems. Here, using the example of normal proliferative monkey kidney (COS) cell monolayers, we investigate global and local topological characteristics of this model system in dependence on its shape. The obtained distributions of cells by their valence demonstrate a difference between the spherical and planar monolayers.

Integration of Cypoviruses into polyhedrin matrix.

Unlike in other viruses, in Cypoviruses the genome is doubly protected since their icosahedral capsids are embedded into a perfect polyhedrin crystal. Current experimental methods cannot resolve the resulting interface structure and we propose a symmetry-based approach to predict it. We reveal a remarkable match between the surfaces of Cypovirus and the outer polyhedrin matrix.

Hidden symmetry of the flavivirus protein shell and pH-controlled reconstruction of the viral surface.

Using recent Zika virus structural data we reveal a hidden symmetry of protein order in immature and mature flavivirus shells, violating the Caspar-Klug paradigmatic model of capsid structures. We show that proteins of the outer immature shell layer exhibit trihexagonal tiling, while proteins from inner and outer layers conjointly form a double-shelled close-packed structure, based on a common triangular spherical lattice. Within the proposed structural model, we furthermore rationalize the structural organization of misassembled non-infectious subviral particles that have no inner capsid.

Packing and trimer-to-dimer protein reconstruction in icosahedral viral shells with a single type of symmetrical structural unit.

Understanding the principles of protein packing and the mechanisms driving morphological transformations in virus shells (capsids) during their maturation can be pivotal for the development of new antiviral strategies. Here, we study how these principles and mechanisms manifest themselves in icosahedral viral capsids assembled from identical symmetric structural units (capsomeres). To rationalize such shells, we model capsomers as symmetrical groups of identical particles interacting with a short-range potential typical of the classic Tammes problem.

Random nature of epithelial cancer cell monolayers.

Although the polygonal shape of epithelial cells has been drawing the attention of scientists for several centuries, only a decade and a half ago it was demonstrated that distributions of polygon types (DOPTs) are similar in proliferative epithelia of many different plant and animal species. In this study, we show that hyper-proliferation of cancer cells disrupts this universal paradigm and results in randomly organized epithelial structures. Examining non-synchronized and synchronized HeLa cervix cells, we suppose that the spread of cell sizes is the main parameter controlling the DOPT in the cancer cell monolayers.

Irreversible and reversible morphological changes in the 6 capsid and similar viral shells: symmetry and micromechanics.

Understanding the physicochemical processes occurring in viruses during their maturation is of fundamental importance since only mature viruses can infect host cells. Here we consider the irreversible and reversible morphological changes that occur with the dodecahedral φ6 procapsid during the sequential packaging of 3 RNA segments forming the viral genome. It is shown that the dodecahedral shape of all the four observed capsid states is perfectly reproduced by a sphere radially deformed by only two irreducible spherical harmonics with icosahedral symmetry and wave numbers l = 6 and l = 10.

Carbon nanotube sorting due to commensurate molecular wrapping.

Single-walled carbon nanotubes (SWCNTs) can be sorted by their structural parameters using organic molecules and polymers: some of which, demonstrating a profound affinity only for specific nanotubes, form dense coatings on them. Here, analyzing well-known examples of flavin group molecules and those of 2,4-dichlorophenoxyacetic acid, we show for the first time that successful formation of the considered coatings depends on the ability of molecules to wrap around the SWCNT in a commensurate way. Commensurability provides a decrease in the free energy of the resulting bilayer system and makes the coating much more stable.

Crystal-like order and defects in metazoan epithelia with spherical geometry.

Since Robert Hooke studied cork cell patterns in 1665, scientists have been puzzled by why cells form such ordered structures. The laws underlying this type of organization are universal, and we study them comparing the living and non-living two-dimensional systems self-organizing at the spherical surface. Such-type physical systems often possess trigonal order with specific elongated defects, scars and pleats, where the 5-valence and 7-valence vertices alternate.

Long-range protein coupling mediated by critical low-energy modes of tubular lipid membranes.

We develop a theory of a resonant effect in protein-membrane coupling taking place in the vicinity of instabilities in tubular lipid membranes (TLMs) under longitudinal force and pressure difference constraints. Two critical low-energy modes defining the stability domain boundaries are found. We show that these modes mediate long-range TLM-protein coupling and interactions between absorbed proteins.