Studying DNA-protein interactions with single-molecule Förster resonance energy transfer

S. Farooq, C. Fijen, J.C. Hohlbein

Research output: Contribution to journalArticleAcademicpeer-review

11 Citations (Scopus)


Single-molecule Förster resonance energy transfer (smFRET) has emerged as a powerful tool for elucidating biological structure and mechanisms on the molecular level. Here, we focus on applications of smFRET to study interactions between DNA and enzymes such as DNA and RNA polymerases. SmFRET, used as a nanoscopic ruler, allows for the detection and precise characterisation of dynamic and rarely occurring events, which are otherwise averaged out in ensemble-based experiments. In this review, we will highlight some recent developments that provide new means of studying complex biological systems either by combining smFRET with force-based techniques or by using data obtained from smFRET experiments as constrains for computer-aided modelling.
Original languageEnglish
Pages (from-to)317-332
Issue number2
Publication statusPublished - 2014


  • rna-polymerase-ii
  • probability-distribution analysis
  • multiparameter fluorescence detection
  • alternating-laser excitation
  • nano-positioning system
  • atomic-force microscope
  • 3.3 angstrom resolution
  • coli rep helicase
  • escherichia-coli
  • structural basis


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