Discovery of coumarin derivatives as fluorescence acceptors for intrinsic fluorescence resonance energy transfer of proteins. Kim, J. H., Sumranjit, J., Kang, H. J., & Chung, S. J. MOLECULAR BIOSYSTEMS, 10(1):30-33, 2014.
doi  abstract   bibtex   
Coumarin analogues were synthezised and evaluated as acceptors for the intrinsic fluorescence resonance energy transfer (iFRET) of tryptophan residues in target proteins. The fluorescence properties such as quantum yields, iFRET efficiencies, and Forster distances of the prepared coumarin analogs were determined in a model system, by their conjugation to biotin, utilizing streptavidin (SAV) as the iFRET donor. The coumarin derivatives reported here represent the most efficient iFRET acceptors for tryptophan, known to date.
@article{ ISI:000327849900004,
Author = {Kim, Ju Hwan and Sumranjit, Jitapa and Kang, Hyo Jin and Chung, Sang J.},
Title = {{Discovery of coumarin derivatives as fluorescence acceptors for
   intrinsic fluorescence resonance energy transfer of proteins}},
Journal = {{MOLECULAR BIOSYSTEMS}},
Year = {{2014}},
Volume = {{10}},
Number = {{1}},
Pages = {{30-33}},
Abstract = {{Coumarin analogues were synthezised and evaluated as acceptors for the
   intrinsic fluorescence resonance energy transfer (iFRET) of tryptophan
   residues in target proteins. The fluorescence properties such as quantum
   yields, iFRET efficiencies, and Forster distances of the prepared
   coumarin analogs were determined in a model system, by their conjugation
   to biotin, utilizing streptavidin (SAV) as the iFRET donor. The coumarin
   derivatives reported here represent the most efficient iFRET acceptors
   for tryptophan, known to date.}},
DOI = {{10.1039/c3mb70323a}},
ISSN = {{1742-206X}},
EISSN = {{1742-2051}},
Unique-ID = {{ISI:000327849900004}},
}

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