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Protein–DNA Interactions: Structure and Energetics

  1. Tom K Kerppola

Published Online: 20 JUN 2001

DOI: 10.1038/npg.els.0001349



How to Cite

Kerppola, T. K. 2001. Protein–DNA Interactions: Structure and Energetics. eLS. .

Author Information

  1. Howard Hughes Medical Institute and University of Michigan Medical School, Ann Arbor, Michigan, USA

Publication History

  1. Published Online: 20 JUN 2001


DNA-binding proteins recognize specific DNA sequences by a combination of molecular interactions. Protein–DNA complex formation is frequently accompanied by conformational changes in one or both components of the complex. Protein–DNA interactions differ in several respects from most other ligand–receptor interactions in cells, and these characteristics place special requirements on the energetics and dynamics of protein–DNA interactions and explain many of the special properties of these complexes.


  • DNA binding specificity;
  • hydrogen bonding;
  • electrostatic interactions;
  • solvation;
  • hydrophobic effect;
  • van der Waal's forces;
  • steric fit;
  • conformational changes;
  • multiprotein complexes;
  • cooperative binding