Paper
14 June 2004 Aggregation of the yellow fluorescent protein zFP538 is pH-dependent
Author Affiliations +
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.
© (2004) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Nadya N Zubova, Leonid M Vinokurov, and Alexander P Savitsky "Aggregation of the yellow fluorescent protein zFP538 is pH-dependent", Proc. SPIE 5329, Genetically Engineered and Optical Probes for Biomedical Applications II, (14 June 2004); https://doi.org/10.1117/12.531480
Advertisement
Advertisement
RIGHTS & PERMISSIONS
Get copyright permission  Get copyright permission on Copyright Marketplace
KEYWORDS
Proteins

Luminescence

Fluorescent proteins

Dynamic light scattering

Lead

Molecular aggregates

Data modeling

Back to Top