Results 21 to 30 of about 15,061 (184)
Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition
Biomolecules, 2014 Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself.
Nataliya Ryabova +3 more
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Frontiers in Microbiology, 2017 Chaperonin GroEL (Cpn60) requires cofactor GroES (Cpn10) for protein refolding in bacteria that possess single groEL and groES genes in a bicistronic groESL operon.
Yue-zhong Li +6 more
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Design and analytical validation of a duplex PCR for Ehrlichia and Rickettsia detection in ticks
Revista Colombiana de Ciencias Pecuarias, 2018 Background: Ehrlichia and Rickettsia are two major rickettsial genera transmitted by ticks that affect a number of wild and domestic animal species and human populations around the world.
Juan C. Pérez Pérez +4 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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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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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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Ligands regulate GroEL thermostability
FEBS Letters, 1997 Escherichia coli heat‐shock proteins GroEL and GroES stimulate (in an ATP‐dependent manner) the folding of various proteins. In this study scanning microcalorimetry was applied to investigate GroEL thermostability in the presence of its ligands. Mg2+ and K+ ions stabilize while ADP destabilizes the GroEL molecule against the action of temperature ...
Surin, A.K +5 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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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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