Hydroxyl radical footprinting of ribosomal proteins on 16S rRNA.

@article{Powers1995HydroxylRF,
  title={Hydroxyl radical footprinting of ribosomal proteins on 16S rRNA.},
  author={Thomas Powers and Harry F. Noller},
  journal={RNA},
  year={1995},
  volume={1 2},
  pages={194-209}
}
Complexes between 16S rRNA and purified ribosomal proteins, either singly or in combination, were assembled in vitro and probed with hydroxyl radicals generated from free Fe(II)-EDTA. The broad specificity of hydroxyl radicals for attack at the ribose moiety in both single- and double-stranded contexts permitted probing of nearly all of the nucleotides in the 16S rRNA chain. Specific protection of localized regions of the RNA was observed in response to assembly of most of the ribosomal… CONTINUE READING