Fluorescence lifetime imaging microscopy (FLIM) to quantify protein-protein interactions inside cells

Rory Duncan

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)


Recent developments in cellular imaging spectroscopy now permit the minimally invasive study of protein dynamics inside living cells. These advances are of interest to cell biologists, as proteins rarely act in isolation, but rather in concert with others in forming cellular machinery. Until recently, all protein interactions had to be determined in vitro using biochemical approaches: this biochemical legacy has provided cell biologists with the basis to test defined protein-protein interactions not only inside cells, but now also with high spatial resolution. These techniques can detect and quantify protein behaviours down to the single-molecule level, all inside living cells. More recent developments in TCSPC (time-correlated single-photon counting) imaging are now also driving towards being able to determine protein interaction rates with similar spatial resolution, and together, these experimental advances allow investigators to perform biochemical experiments inside living cells.

Original languageEnglish
Pages (from-to)679-682
Number of pages4
JournalBiochemical Society Transactions
Issue number5
Publication statusPublished - Oct 2006


  • Fluorescence Resonance Energy Transfer
  • Fluorescent Antibody Technique
  • Image Processing, Computer-Assisted
  • Microscopy
  • Proteins
  • Fluorescence


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