Application of fluorescence resonance energy transfer in protein studies

Linlin Ma, Fan Yang, Jie Zheng

Research output: Contribution to journalArticlepeer-review

62 Scopus citations


Since the physical process of fluorescence resonance energy transfer (FRET) was elucidated more than six decades ago, this peculiar fluorescence phenomenon has turned into a powerful tool for biomedical research due to its compatibility in scale with biological molecules as well as rapid developments in novel fluorophores and optical detection techniques. A wide variety of FRET approaches have been devised, each with its own advantages and drawbacks. Especially in the last decade or so, we are witnessing a flourish of FRET applications in biological investigations, many of which exemplify clever experimental design and rigorous analysis. Here we review the current stage of FRET methods development with the main focus on its applications in protein studies in biological systems, by summarizing the basic components of FRET techniques, most established quantification methods, as well as potential pitfalls, illustrated by example applications.

Original languageEnglish (US)
Pages (from-to)87-100
Number of pages14
JournalJournal of Molecular Structure
StatePublished - Dec 5 2014


  • Assembly
  • Fluorophore
  • FRET
  • Microscopy
  • Protein
  • Spectroscopy

ASJC Scopus subject areas

  • Spectroscopy
  • Analytical Chemistry
  • Inorganic Chemistry
  • Organic Chemistry


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