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A New Sensitive Photochemical Technique for Detection of Fluorescence Resonance Energy Transfer

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Spectroscopy of Biological Molecules
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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.

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References

  1. Stryer, L.: Fluorescence energy transfer as a spectroscopic ruler, Annu. Rev. Biochem. 47 (1978) 819–846.

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  2. 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.

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  3. Wu, P., and Brand, L.: Resonance energy transfer: methods and application, Anal. Biochem. 218 (1994), 1–13.

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  4. Mekler, V.M. A photochemical technique to enhance sensitivity of detection of fluorescence resonance energy transfer, Photochem. Photobiol. 59 (1994), 615–620.

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© 1995 Springer Science+Business Media Dordrecht

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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

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  • 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

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