Paper
12 September 2003 Oligomerizations strongly influences the brightness of DsRed fluorescence
Anastasiya Yu. Bulavina, Gerry McDermott, Evgenia G. Matveeva, Alexander P. Savitsky
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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.
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Anastasiya Yu. Bulavina, Gerry McDermott, Evgenia G. Matveeva, and Alexander P. Savitsky "Oligomerizations strongly influences the brightness of DsRed fluorescence", Proc. SPIE 4967, Genetically Engineered and Optical Probes for Biomedical Applications, (12 September 2003); https://doi.org/10.1117/12.479830
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KEYWORDS
Luminescence

Proteins

Polarization

Green fluorescent protein

Dynamic light scattering

Fluorescent proteins

Molecules

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