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Peculiarities of the Super-Folder GFP Folding in a Crowded Milieu

Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., St. Petersburg 194064, Russia
Institute of Physics, Nanotechnology and Telecommunications, Peter the Great St. Petersburg State Polytechnic University, 29 Polytechnicheskaya st., St. Petersburg 195251, Russia
Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd. MDC07, Tampa, FL 33612, USA
Authors to whom correspondence should be addressed.
Academic Editor: Salvador Ventura
Int. J. Mol. Sci. 2016, 17(11), 1805;
Received: 26 August 2016 / Revised: 11 October 2016 / Accepted: 20 October 2016 / Published: 28 October 2016
(This article belongs to the Collection Protein Folding)
The natural cellular milieu is crowded by large quantities of various biological macromolecules. This complex environment is characterized by a limited amount of unoccupied space, limited amounts of free water, and changed solvent properties. Obviously, such a tightly packed cellular environment is poorly mimicked by traditional physiological conditions, where low concentrations of a protein of interest are analyzed in slightly salted aqueous solutions. An alternative is given by the use of a model crowded milieu, where a protein of interest is immersed in a solution containing high concentrations of various polymers that serve as model crowding agents. An expected outcome of the presence of such macromolecular crowding agents is their ability to increase conformational stability of a globular protein due to the excluded volume effects. In line with this hypothesis, the behavior of a query protein should be affected by the hydrodynamic size and concentration of an inert crowder (i.e., an agent that does not interact with the protein), whereas the chemical nature of a macromolecular crowder should not play a role in its ability to modulate conformational properties. In this study, the effects of different crowding agents (polyethylene glycols (PEGs) of various molecular masses (PEG-600, PEG-8000, and PEG-12000), Dextran-70, and Ficoll-70) on the spectral properties and unfolding–refolding processes of the super-folder green fluorescent protein (sfGFP) were investigated. sfGFP is differently affected by different crowders, suggesting that, in addition to the expected excluded volume effects, there are some changes in the solvent properties. View Full-Text
Keywords: super-folder GFP; protein folding; conformational stability; crowded milieu; excluded volume effect; solvent properties super-folder GFP; protein folding; conformational stability; crowded milieu; excluded volume effect; solvent properties
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MDPI and ACS Style

Stepanenko, O.V.; Stepanenko, O.V.; Kuznetsova, I.M.; Uversky, V.N.; Turoverov, K.K. Peculiarities of the Super-Folder GFP Folding in a Crowded Milieu. Int. J. Mol. Sci. 2016, 17, 1805.

AMA Style

Stepanenko OV, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Peculiarities of the Super-Folder GFP Folding in a Crowded Milieu. International Journal of Molecular Sciences. 2016; 17(11):1805.

Chicago/Turabian Style

Stepanenko, Olesya V., Olga V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, and Konstantin K. Turoverov 2016. "Peculiarities of the Super-Folder GFP Folding in a Crowded Milieu" International Journal of Molecular Sciences 17, no. 11: 1805.

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