Radiolytic protein surface mapping

Douglas P. Greiner, Karin A. Hughes, Claude F. Meares

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


We report that high energy beta particles may function as a means for mapping the surface of a protein. Comparable to Fe-EDTA in the presence of ascorbate and peroxide, 90Y-EDTA alone can break polypeptide backbone bonds on the surface of E. coli RNA polymerase. The two methods give very similar fragmentation patterns, although some unique fragments are produced by each. Radiolytic footprinting may prove useful for mapping proteins inside living cells, since beta-radiolysis produces reactive species up to ≃ 1 cm away from the emitting 90Y.

Original languageEnglish (US)
Pages (from-to)1006-1008
Number of pages3
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Aug 23 1996

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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