Electrophoretic analysis of multiple protein-DNA interactions

Michael G. Fried, Margaret A. Daugherty

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

Under favorable conditions, native gel electrophoresis allows the resolution of protein-DNA complexes that differ in stoichiometry, identities of occupied DNA sequences (configuration), and macromolecular conformation. This technique provides a unique opportunity to analyze, in thermodynamic terms, the molecular interactions that govern the equilibrium distributions of species in protein-DNA mixtures. Here we describe a general theoretical approach to the analysis of electrophoretic band intensities, and provide examples of its application to the analysis of several interacting systems.

Original languageEnglish
Pages (from-to)1247-1253
Number of pages7
JournalElectrophoresis
Volume19
Issue number8-9
DOIs
StatePublished - Jun 1998

Keywords

  • Mobility-shift assay
  • Protein-DNA interactions
  • Thermodynamics

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry

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