Intermolecular Interactions in a Two-Layered Viral Capsid That Requires a Complex Symmetry Mismatch
نویسندگان
چکیده
منابع مشابه
Breaking the symmetry of a viral capsid.
The small size, and thus coding capacity, of viral genomes necessitates the repetitive use of identical building blocks in constructing the viral capsid. This genetic economy gives rise to highly symmetric structures, typically with either helical or icosahedral geometries. Assembly of symmetric viral capsids is believed to proceed via “conformational switching” of individual protein subunits (...
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15 صفحه اولRetrovirus restriction by TRIM5 proteins requires recognition of only a small fraction of viral capsid subunits.
The host restriction factors TRIM5α and TRIMCyp potently inhibit retrovirus infection by binding to the incoming retrovirus capsid. TRIM5 proteins are dimeric, and their association with the viral capsid appears to be enhanced by avidity effects owing to formation of higher-order oligomeric complexes. We examined the stoichiometric requirement for TRIM5 functional recognition by quantifying the...
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Intermolecular interactions in cyclometalated Ru complex dye (FT89) dimers, carbazole organic dye (MK-45 and MK-111) dimers, FT89-MK-45 complexes, and FT89-MK-111 complexes were investigated using density functional theory (DFT) and time-dependent DFT (TD-DFT) to elucidate the improvement mechanism of dye-sensitized solar cell (DSSC) performance due to cosensitization with FT89 and MK dyes. All...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 2003
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.77.20.11114-11124.2003