Chaperones play a vital role in the life of cells by facilitating the correct folding of other proteins and maintaining them in a functional state, being themselves, as a rule, more stable than the rest of cell proteins. Their functional properties naturally tempt investigators to actively adapt them for biotechnology needs. This review will mostly focus on the applications found for the bacterial chaperonin GroE and its counterparts from other organisms, in biotechnology or for research purposes, both in their engineered or intact versions.
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| http://dx.doi.org/10.3390/biom12050607 | DOI Listing |
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GroEL-A Versatile Chaperone for Engineering and a Plethora of Applications.
Biomolecules
April 2022
Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences. 33, Bld. 2 Leninsky Ave., Moscow 119071, Russia.
Chaperones play a vital role in the life of cells by facilitating the correct folding of other proteins and maintaining them in a functional state, being themselves, as a rule, more stable than the rest of cell proteins. Their functional properties naturally tempt investigators to actively adapt them for biotechnology needs. This review will mostly focus on the applications found for the bacterial chaperonin GroE and its counterparts from other organisms, in biotechnology or for research purposes, both in their engineered or intact versions.
View Article and Find Full Text PDFThe Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms.
Front Mol Biosci
May 2018
Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, United States.
The nucleotide-free chaperonin GroEL is capable of capturing transient unfolded or partially unfolded states that flicker in and out of existence due to large-scale protein dynamic vibrational modes. In this work, three short vignettes are presented to highlight our continuing advances in the application of GroEL biosensor biolayer interferometry (BLI) technologies and includes expanded uses of GroEL as a molecular scaffold for electron microscopy determination. The first example presents an extension of the ability to detect dynamic pre-aggregate transients in therapeutic protein solutions where the assessment of the kinetic stability of any folded protein or, as shown herein, quantitative detection of mutant-type protein when mixed with wild-type native counterparts.
View Article and Find Full Text PDFThe versatile mutational "repertoire" of Escherichia coli GroEL, a multidomain chaperonin nanomachine.
Biophys Rev
April 2018
Graduate School of Engineering and Graduate School of Medical Sciences, Tottori University, Tottori, 680-8552, Japan.
The bacterial chaperonins are highly sophisticated molecular nanomachines, controlled by the hydrolysis of ATP to dynamically trap and remove from the environment unstable protein molecules that are susceptible to denaturation and aggregation. Chaperonins also act to assist in the refolding of these unstable proteins, providing a means by which these proteins may return in active form to the complex environment of the cell. The Escherichia coli GroE chaperonin system is one of the largest protein supramolecular complexes known, whose quaternary structure is required for segregating aggregation-prone proteins.
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