Measuring protein conformational changes by FRET/LRET

Curr Opin Biotechnol. 2002 Aug;13(4):292-6. doi: 10.1016/s0958-1669(02)00332-4.


Fluorescence resonance energy transfer (FRET) provides a unique means of measuring interatomic distances in biological molecules in real time. Recent advances have been made in the application of this technique to studies of conformational changes in proteins. New ways of introducing fluorescence probes into proteins, newly developed fluorescence probes, and progress in the technologies for fluorescence signal detection have greatly expanded the range of applications of FRET. In particular, studies of conformational changes in proteins at a single molecule level and in the native in vivo context of a living cell are now possible.

Publication types

  • Review

MeSH terms

  • Fluorescence Resonance Energy Transfer / methods*
  • Fluorescence Resonance Energy Transfer / trends*
  • Fluorescent Dyes / chemistry*
  • Molecular Probes / chemistry
  • Motion
  • Protein Conformation*
  • Proteins / chemistry*
  • Staining and Labeling / methods*


  • Fluorescent Dyes
  • Molecular Probes
  • Proteins