Display Settings:


Send to:

Choose Destination
See comment in PubMed Commons below
Curr Opin Biotechnol. 2002 Aug;13(4):292-6.

Measuring protein conformational changes by FRET/LRET.

Author information

  • 1E.A. Doisy Department of Biochemistry and Molecular Biology, St Louis University School of Medicine, 1402 South Grand Blvd, St Louis, MO 63104, USA. heydukt@slu.edu


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.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk