ArticlePloS one2014
Sensitivity of superfolder GFP to ionic agents.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Protein degradation kinetics measured by microinjection and live-cell fluorescence microscopy.Scientific reports · 2024Article
- Chemically stable fluorescent proteins for advanced microscopy.Nature methods · 2022Article
- LSSmScarlet2 and LSSmScarlet3, Chemically Stable Genetically Encoded Red Fluorescent Proteins with a Large Stokes' Shift.International journal of molecular sciences · 2022Article
- GEM-IL: A highly responsive fluorescent lactate indicator.Cell reports methods · 2021Article
- mGreenLantern: a bright monomeric fluorescent protein with rapid expression and cell filling properties for neuronal imaging.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Improved GFP Variants to Study Gene Expression in Haloarchaea.Frontiers in microbiology · 2019Article
- The Pathways of the iRFP713 Unfolding Induced by Different Denaturants.International journal of molecular sciences · 2018Article
- Peculiarities of the Super-Folder GFP Folding in a Crowded Milieu.International journal of molecular sciences · 2016Article
- Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms.PeerJ · 2016Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Superfolder variant of the green fluorescent protein (sfGFP) became a favorite probe for examination of the unfolding-refolding processes of fluorescent proteins with beta-barrel structure owing to its reversible unfolding in comparison with other fluorescent proteins. Its benefit is the proper folding even in fusion constructions with poorly folded polypeptides. We noticed that guanidine thiocyanate affects not only the structure of protein but its chromophore directly. Therefore we studied the influence of ionic denaturants and salts including guanidine thiocyanate, guanidine hydrochloride, sodium chloride and sodium thiocyanate on spectral features of sfGFP. It was shown that moderate amounts of the studied agents do not disrupt sfGFP structure but provoke pronounced alteration of its spectral characteristics. Changes in absorption and CD spectra in visible spectral range indicate the specific binding of SCN- and Cl- anions in the sfGFP chromophore vicinity. The anion binding results in the redistribution of sfGFP molecules with neutral and anionic chromophores. This also hinders the proton transfer in the chromophore excited state, considerably decreasing the fluorescence intensity of sfGFP. Our results indicate that when ionic denaturants are used in the studies of fluorescent protein folding their effect on fluorophore charge state should be taken into account.
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