Abstract
Fluorescence resonance energy transfer (FRET) between labeled macromolecules or probes has been widely used to study the structure of proteins, membranes and nucleic acids [1–3]. The FRET efficiency (ω) was usually determined from fluorescence quenching of an energy donor or the sensitization of an energy acceptor fluorescence. Background processes usually result in that the low limit of reliable detection of ω is about 0.05. When the donor-acceptor distance is more than 8 nm similar sensitivity is inadequate.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Stryer, L.: Fluorescence energy transfer as a spectroscopic ruler, Annu. Rev. Biochem. 47 (1978) 819–846.
Fairclough, R.H. and Cantor, C.L.: The use of singlet- singlet energy transfer to study macromolecular assembles, in Ch. W. Hirs and S.N. Timasheff (eds.), Methods in Enzymology, Academic Press, London, 48 (1978), 347–379.
Wu, P., and Brand, L.: Resonance energy transfer: methods and application, Anal. Biochem. 218 (1994), 1–13.
Mekler, V.M. A photochemical technique to enhance sensitivity of detection of fluorescence resonance energy transfer, Photochem. Photobiol. 59 (1994), 615–620.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Mekler, V.M. (1995). A New Sensitive Photochemical Technique for Detection of Fluorescence Resonance Energy Transfer. In: Merlin, J.C., Turrell, S., Huvenne, J.P. (eds) Spectroscopy of Biological Molecules. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-0371-8_6
Download citation
DOI: https://doi.org/10.1007/978-94-011-0371-8_6
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-4166-9
Online ISBN: 978-94-011-0371-8
eBook Packages: Springer Book Archive