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Proceedings Paper

Aggregation of the yellow fluorescent protein zFP538 is pH-dependent
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Paper Abstract

pH-dependent aggregation and dissociation of yellow fluorescent protein zFP538 were studied by gel-filtration, dynamic light scattering, and fluorescence spectroscopy. According to the gel-filtration data for low concentration of zFP538 the molecular weight of aggregates decreases upon changing pH from alkaline to neutral. Dynamic light scattering showed that zFP538 aggregates strongly in concentrated solutions. Aggregation influences heavily the pH-profile of fluorescence of zFP538 and stabilizes zFP538 against fluorescence quenching on acidification. Reduction of the protein concentration results in the shifting of pH profile to the alkaline region. Conclusion: aggregation of the yellow fluorescent protein zFP538 depends on pH; dilution of the protein solution is accompanied by dissociation of zFP538 aggregates under neutral and alkaline pH.

Paper Details

Date Published: 14 June 2004
PDF: 5 pages
Proc. SPIE 5329, Genetically Engineered and Optical Probes for Biomedical Applications II, (14 June 2004); doi: 10.1117/12.531480
Show Author Affiliations
Nadya N Zubova, M.V. Lomonosov Moscow State Univ. (Russia)
Leonid M Vinokurov, Institute of Bioorganic Chemistry (Russia)
Alexander P Savitsky, M.V. Lomonosov Moscow State Univ. and Institute of Biochemistry (Russia)


Published in SPIE Proceedings Vol. 5329:
Genetically Engineered and Optical Probes for Biomedical Applications II
Alexander P. Savitsky; Darryl J. Bornhop; Ramesh Raghavachari; Samuel I. Achilefu, Editor(s)

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