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- W1763144417 endingPage "325" @default.
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- W1763144417 abstract "The structure of tobacco mosaic virus (TMV) has been determined by fiber diffraction methods at 2.9 A resolution, and refined by restrained least-squares to an R-factor of 0.096. Protein-nucleic acid interactions are clearly visible. The final model contains all of the non-hydrogen atoms of the RNA and the protein, 71 water molecules, and two calcium-binding sites. Viral disassembly is driven by electrostatic repulsions between the charges in two carboxyl-carboxylate pairs and a phosphate-carboxylate pair. The phosphate-carboxylate pair and at least one of the carboxyl-carboxylate pairs appear to be calcium-binding sites. Nucleotide specificity, enabling TMV to recognize its own RNA by a repeating pattern of guanine residues, is provided by two guanine-specific hydrogen bonds in one of the three base-binding sites." @default.
- W1763144417 created "2016-06-24" @default.
- W1763144417 creator A5025152584 @default.
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- W1763144417 date "1989-07-01" @default.
- W1763144417 modified "2023-10-14" @default.
- W1763144417 title "Visualization of protein-nucleic acid interactions in a virus" @default.
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- W1763144417 doi "https://doi.org/10.1016/0022-2836(89)90391-4" @default.
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