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- W2068011674 abstract "A proposed conformation for the TMV protein presents the subunit as a hexagonal plate with the amide linkages all located on one surface (the “hydrophilic” surface) and the side chains located on the opposite (or “hydrophobic”) surface of the plate. On the “hydrophilic” surface of the proposed subunit, the carbonyl oxygens of the peptide bonds are placed at the corners of small regular hexagons arranged in a honeycomb pattern. This honeycomb pattern is dimensionally and figuratively similar to a plane of “second neighbor” water oxygens. Starting with the carbonyl oxygen of the N-terminal acetyl group, the 159 carbonyl oxygens of the TMV protein subunit follow an expanding spiral in the pattern to fill the corner positions of 65 of the honeycomb cells. Since these cells have a side length equivalent to about 4.8 Å, the overall subunit dimensions can be calculated. By numbering the positions of the carbonyl oxygens along the path of the primary chain sequence, the position of side chains in the subunit can be determined approximately. A large number of the TMV protein subunits were laid out on calibrated hexagonally ruled paper, and the resulting patterns were used as models to study possible axial and equatorial subunit interactions. Six of the subunits were assembled in three pairs to produce a unit which fulfills quite exactly the cross-sectional dimensions of the TMV protein rod. The forces postulated for holding these six subunits together are the many carboxyl-carboxamide, carboxyl-carboxyl, and hydroxyl-carboxamide side chain interactions which the models indicate can probably occur. The resulting combination of six subunits has been suggested as a model for the A-protein of TMV. By further studying the axial and equatorial overlap of the A-protein models, possible explanations for the radial density pattern and axial repeat dimensions of TMV protein have been presented." @default.
- W2068011674 created "2016-06-24" @default.
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- W2068011674 date "1964-01-01" @default.
- W2068011674 modified "2023-10-14" @default.
- W2068011674 title "Molecular models: IV. A suggested conformation for the protein subunit of tobacco mosaic virus" @default.
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- W2068011674 doi "https://doi.org/10.1016/0022-5193(64)90068-2" @default.
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