Structure of Tobacco Mosaic Virus

@article{Franklin1955StructureOT,
  title={Structure of Tobacco Mosaic Virus},
  author={Rosalind E. Franklin},
  journal={Nature},
  year={1955},
  volume={175},
  pages={379-381}
}
  • R. Franklin
  • Published 26 February 1955
  • Chemistry, Medicine
  • Nature
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References

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Prolin als Endgruppe des Tabakmosaikvirus
Das nucleinsäurefreie Protein des Tabakmosaikvirus wurde mit Dinitrofluorbenzol umgesetzt und hydrolysiert. Bei vollständiger Hydrolyse ist kein α-Dinitrophenyl-Derivat einer Aminosäure faßbar,
High-resolution electron microscopy of the particles of tobacco mosaic virus.
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    Biochimica et biophysica acta
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Infra-Red Dichroism and Protein Structure: Infra-Red Dichroism of Tobacco Mosaic Virus Nucleoprotein
TLDR
The infra-Red dichroism of Tobacco Mosaic Virus Nucleoprotein is related to the structure of the Tournaisian virus and its role in cell reprograming is unclear.
The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain.
TLDR
This work has used information about interatomic distances, bond angles, and other configurational parameters to construct two reasonable hydrogen-bonded helical configurations for the polypeptide chain; it is likely that these configurations constitute an important part of the structure of both fibrous and globular proteins, as well as of syntheticpolypeptides.
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