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Hydroxyl Radical Interference

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DNA-Protein Interactions

Part of the book series: Methods in Molecular Biology ((MIMB,volume 148))

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Abstract

Interference studies are just the inverse approach of “footprinting” experiments. In one type of experiment, the effect of a chemical modification of a single base on the subsequent binding of a sequence-specific protein is determined, whereas in the other, it is the accessibility of the protein-bound DNA to modification that is determined. Thus, the experiments necessarily differ in the order in which the protein binding and DNA modification steps occur. The “interference” approach is characterized first by chemical modification of the DNA and by subsequent protein binding. Such studies provide information on the change of the binding strength following single-base modification. This change can either be positive or negative and can be quantified by the gel shift assay (1) (see Chapters 2 and 5).

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References

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© 2001 Humana Press Inc., Totowa, NJ

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Schickor, P., Zaychikov, E., Heumann, H. (2001). Hydroxyl Radical Interference. In: Moss, T. (eds) DNA-Protein Interactions. Methods in Molecular Biology, vol 148. Humana Press. https://doi.org/10.1385/1-59259-208-2:245

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  • DOI: https://doi.org/10.1385/1-59259-208-2:245

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-625-3

  • Online ISBN: 978-1-59259-208-1

  • eBook Packages: Springer Protocols

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