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Proceedings Paper

Oligomerization strongly influences the brightness of DsRed fluorescence
Author(s): Anastasiya Yu. Bulavina; Gerry McDermott; Evgenia G. Matveeva; Alexander P. Savitsky
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Paper Abstract

The red fluorescent protein DsRed (drFP583), has become an excellent addition to Green Fluorescent Protein (GFP) and its mutants in biological and biotechnical applications due to the significantly red-shifted emission maximum at 583 nm. However, the use of DsRed is complicated by its oligomerization. According to the data from dynamic light scattering, steady-state fluorescence polarization, DsRed and its no-aggregated mutants are organized as tetramers in concentrated solutions. But at the concentration of 10-8-10-9 M fluorescence polarization shows the existence of the monomeric form of DsRed. Neither dimer nor trimer forms of DsRed were detected. Upon dilution of concentrated solutions of DsRed, the intensity of fluorescence decreased with time. Observed fluorescence kinetics fits well to the tetramer - monomer transition. The brightness of the monomeric form of DsRed was suggested to be significantly less compared to the tetrameric form.

Paper Details

Date Published: 12 September 2003
PDF: 10 pages
Proc. SPIE 4967, Genetically Engineered and Optical Probes for Biomedical Applications, (12 September 2003); doi: 10.1117/12.479830
Show Author Affiliations
Anastasiya Yu. Bulavina, M.V. Lomonosov Moscow State Univ. (Russia)
Gerry McDermott, Lawrence Berkeley National Lab. (United States)
Evgenia G. Matveeva, A.N. Bach Institute of Biochemistry (Russia)
Alexander P. Savitsky, A.N. Bach Institute of Biochemistry (Russia)

Published in SPIE Proceedings Vol. 4967:
Genetically Engineered and Optical Probes for Biomedical Applications
Darryl J. Bornhop; Ramesh Raghavachari; Samuel I. Achilefu; Alexander P. Savitsky, Editor(s)

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