PMID: 11332886May 3, 2001Paper

Protein flexibility as revealed by fluorescence resonance energy transfer: an extension of the method for systems with multiple labels

Journal of Photochemistry and Photobiology. B, Biology
B SomogyiM Nyitrai

Abstract

The temperature profile of the normalized fluorescence resonance energy transfer efficiency is capable of monitoring the relative change of flexibility and/or conformational state of macromolecules [Biochemistry 23 (1984) 3403]. The method described earlier for one donor-one acceptor systems is extended to multiple fluorophore systems when the energy transfer occurs between either one donor-m acceptors, or n donors-one acceptor or n donors-m acceptors (where n and m are integer values). It is shown that the normalized energy transfer efficiency obtained for systems containing multiple labels is a linear combination of the normalized transfer efficiency assigned to individual donor-acceptor pairs of the system, thus its temperature profile is capable of monitoring the change of intramolecular flexibility and/or conformational state.

References

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Jan 1, 1970·Proceedings of the National Academy of Sciences of the United States of America·K Beardsley, C R Cantor
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Citations

Sep 13, 2008·Journal of Medicinal Chemistry·Pietro CozziniChristoph A Sotriffer
Dec 5, 2003·European Journal of Biochemistry·Emoke BódisBéla Somogyi
Jul 4, 2012·The Journal of Biological Chemistry·Zoltán UjfalusiBeáta Bugyi
Feb 24, 2006·The Journal of Biological Chemistry·Beáta BugyiMiklós Nyitrai
Apr 1, 2010·Expert Opinion on Drug Discovery·Christian Beier, Martin Zacharias
Oct 22, 2008·Biophysical Journal·Zoltán UjfalusiMiklós Nyitrai

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