Electrophoretic analysis of multiple protein-DNA interactions

Electrophoresis. 1998 Jun;19(8-9):1247-53. doi: 10.1002/elps.1150190804.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Cyclic AMP Receptor Protein / metabolism*
  • DNA, Bacterial / metabolism*
  • DNA-Binding Proteins / metabolism*
  • Electrophoresis, Polyacrylamide Gel / methods*
  • Protein Binding

Substances

  • Bacterial Proteins
  • Cyclic AMP Receptor Protein
  • DNA, Bacterial
  • DNA-Binding Proteins