Mapping protein-ligand interactions by hydroxyl-radical protein footprinting.

@article{Loizos2004MappingPI,
  title={Mapping protein-ligand interactions by hydroxyl-radical protein footprinting.},
  author={Nick Loizos},
  journal={Methods in molecular biology},
  year={2004},
  volume={261},
  pages={199-210}
}
  • Nick Loizos
  • Published 2004 in Methods in molecular biology
Hydroxyl-radical protein footprinting is a direct method to map protein sites involved in macromolecular interactions. The first step is to radioactively end-label the protein. Using hydroxyl radicals as a peptide backbone cleavage reagent, the protein is then cleaved in the absence and presence of ligand. Cleavage products are separated by high-resolution gel electrophoresis. The digital image of the footprinting gel can be subjected to quantitative analysis to identify changes in the… CONTINUE READING