The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo

Curr Opin Struct Biol. 2001 Oct;11(5):573-8. doi: 10.1016/s0959-440x(00)00249-9.


Intermolecular and intramolecular FRET between two spectrally overlapping green fluorescent protein variants fused to two different host proteins or at two different sites within the same protein offers a unique opportunity to monitor real-time protein-protein interactions or protein conformational changes. By using fluorescence digital imaging microscopy, one can visualize the location of green fluorescent proteins within a living cell and follow the time course of the changes in FRET corresponding to cellular events at a millisecond time resolution. The observation of such dynamic molecular events in vivo provides vital insight into the action of biological molecules.

Publication types

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

MeSH terms

  • Calcium Signaling
  • Endopeptidases / metabolism
  • Green Fluorescent Proteins
  • Luminescent Proteins / chemistry
  • Luminescent Proteins / genetics
  • Macromolecular Substances
  • Microscopy, Fluorescence / methods*
  • Phosphorylation
  • Protein Conformation
  • Proteins / chemistry*


  • Luminescent Proteins
  • Macromolecular Substances
  • Proteins
  • Green Fluorescent Proteins
  • Endopeptidases