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Abstract
Förster resonance energy transfer between 7-amino-4-methyl-3-coumarinylacetic acid, (AMCA, donor) and 5- carboxytetramethylrhodamine, (TAMRA, acceptor) bound to Lys(AMCA)-Gly-Pro-Arg-Ser-Leu-Ser-Gly-Lys (TAMRA)-NH2 peptide is demonstrated by various spectroscopic techniques in glycerol at room temperature. In particular, nonexponential character of fluorescence intensity decay evidences the distance distribution between the donor and acceptor sites resulting from the flexibility of the peptide. Numerical analysis of the fluorescence decay yields the distance distribution parameters. The results obtained are consistent with those obtained from steady-state fluorescence indicating that energy transfer is more efficient than suggested by the relation between the critical distance and donor-acceptor distance for elongated peptide conformation.
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Authors (10)
-
Anna Synak
-
R. Fudala
-
Ignacy Gryczynski
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S Shah
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Illia E. Serdiuk
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Beata Grobelna
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P Arłukowicz
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Aleksander Kubicki
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Piotr Bojarski
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Details
- Category:
- Articles
- Type:
- artykuł w czasopiśmie wyróżnionym w JCR
- Published in:
-
DYES AND PIGMENTS
no. 158,
pages 60 - 64,
ISSN: 0143-7208 - Language:
- English
- Publication year:
- 2018
- Bibliographic description:
- Synak A., Fudala R., Gryczynski I., Kułak L., Shah S., Serdiuk I., Grobelna B., Arłukowicz P., Kubicki A., Bojarski P.: AMCA to TAMRA long range resonance energy transfer on a flexible peptide// DYES AND PIGMENTS. -Vol. 158, (2018), s.60-64
- DOI:
- Digital Object Identifier (open in new tab) 10.1016/j.dyepig.2018.05.019
- Verified by:
- Gdańsk University of Technology
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