Results 31 to 40 of about 18,538 (219)
Molecules, 2023 The incorporation of photoproteins into proteins of interest allows the study of either their localization or intermolecular interactions in the cell.
Victor Marchenkov +8 more
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The Chaperonin GroEL Is Destabilized by Binding of ADP [PDF]
Journal of Biological Chemistry, 1995 The urea-induced dissociation and subsequent conformational transitions of the nucleotide-bound form of GroEL were studied by light scattering, 4,4'-bis(1-anilino-8- naphthalenesulfonic acid) binding, and intrinsic tyrosine fluorescence. Magnesium ion alone (10 mM) stabilizes GroEL and leads to coordination of the structural transitions monitored by ...
B M, Gorovits, P M, Horowitz
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Probing the functional mechanism of Escherichia coli GroEL using circular permutation. [PDF]
PLoS ONE, 2011 BACKGROUND: The Escherichia coli chaperonin GroEL subunit consists of three domains linked via two hinge regions, and each domain is responsible for a specific role in the functional mechanism.
Tomohiro Mizobata +5 more
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Biomolecules, 2021 Group I chaperonins are a highly conserved family of essential proteins that self-assemble into molecular nanoboxes that mediate the folding of cytoplasmic proteins in bacteria and organelles.
Karla N. Valenzuela-Valderas +3 more
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A structural model for GroEL–polypeptide recognition [PDF]
Proceedings of the National Academy of Sciences, 1997 A monomeric peptide fragment of GroEL, consisting of residues 191–376, is a mini-chaperone with a functional chaperoning activity. We have solved the crystal structure at 1.7 Å resolution of GroEL(191–376) with a 17-residue N-terminal tag. The N-terminal tag of one molecule binds in the active site of a neighboring molecule in the crystal. This appears
A M, Buckle, R, Zahn, A R, Fersht
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Mechanisms involved in the functional divergence of duplicated GroEL chaperonins in Myxococcus xanthus DK1622. [PDF]
PLoS Genetics, 2013 The gene encoding the GroEL chaperonin is duplicated in nearly 30% of bacterial genomes; and although duplicated groEL genes have been comprehensively determined to have distinct physiological functions in different species, the mechanisms involved have ...
Yan Wang +9 more
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GroEL-Proteotyping of Bacterial Communities Using Tandem Mass Spectrometry
, 2023 Profiling bacterial populations in mixed communities is a common task in microbiology. Sequencing of 16S small subunit ribosomal-RNA (16S rRNA) gene amplicons is a widely accepted and functional approach but relies on amplification primers and cannot ...
Myriel Cooper +4 more
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Biomolecules, 2020 The main events in chaperone-assisted protein folding are the binding and ligand-induced release of substrate proteins. Here, we studied the location of denatured proteins previously bound to the GroEL chaperonin resulting from the action of the GroES co-
Victor Marchenkov +4 more
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Frontiers in Molecular Biosciences, 2023 Protein folding is often hampered by intermolecular protein aggregation, which can be prevented by a variety of chaperones in the cell. Bacterial chaperonin GroEL is a ring-shaped chaperone that forms complexes with its cochaperonin GroES, creating ...
Hideki Taguchi, Ayumi Koike-Takeshita
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