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September 1, 1984Journal of Biological ChemistryOpen Access

Photochemical cross-linking of the Escherichia coli single-stranded DNA-binding protein to oligodeoxynucleotides. Identification of phenylalanine 60 as the site of cross-linking.

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Authors

BMB M MerrillResearch Triangle Park FoundationKWKenneth R. WilliamsHouston MethodistJCJohn W. ChaseBoston University

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Merrill et al. (1984) studied this question.

synapsesocial.com/papers/6a6f42bca528af2d65c2e6d8https://doi.org/10.1016/s0021-9258(18)90591-0
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Photoinduced crosslinkage, in situ, of Escherichia coli 30S ribosomal proteins to 16S rRNA: identification of crosslinked proteins and relations between reactivity and ribosome structure1976 · 40 citations
  2. 2Proteins of the 30‐S Subunit of Escherichia coli Ribosomes which Interact Directly with Natural mRNA1983 · 16 citations
  3. 3Studies on polynucleotides. 146. High-pressure liquid chromatography in polynucleotide synthesis1978 · 187 citations
  4. 4Characterization of the Escherichia coli SSB-113 mutant single-stranded DNA-binding protein. Cloning of the gene, DNA and protein sequence analysis, high pressure liquid chromatography peptide mapping, and DNA-binding studies.1984 · 93 citations
  5. 5Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins.1983 · 202 citations