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Detection of a new bla<sub>OXA-51-Like</sub> variant (bla<sub>OXA-1328</sub>) and a novel sequence type (ST3457/2790) in Acinetobacter baumannii isolated from community sewage and an incinerator surface in Nigeria. [PDF]
BMC Res NotesSaleh KJ +5 more
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Origin of chaperone dependence and assembly complexity in Rubisco’s biogenesis
Ng JZY +7 more
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Chaperonin Mechanisms: Multiple and (Mis)Understood?
Annual Review of Biophysics, 2022The chaperonins are ubiquitous and essential nanomachines that assist in protein folding in an ATP-driven manner. They consist of two back-to-back stacked oligomeric rings with cavities in which protein (un)folding can take place in a shielding ...
A. Horovitz +3 more
semanticscholar +1 more source
Journal of Chromatography B: Biomedical Sciences and Applications, 1999
The availability of protein samples of sufficient quality and in sufficient quantity is a driving force in biology and biotechnology. Protein samples that are free of critical contaminants are required for specific assays. Large amounts of highly homogeneous and reproducible material are needed for crystallography and nuclear magnetic resonance studies
E, Quaite-Randall, A, Joachimiak
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The availability of protein samples of sufficient quality and in sufficient quantity is a driving force in biology and biotechnology. Protein samples that are free of critical contaminants are required for specific assays. Large amounts of highly homogeneous and reproducible material are needed for crystallography and nuclear magnetic resonance studies
E, Quaite-Randall, A, Joachimiak
openaire +2 more sources
Chaperonin: Co-chaperonin Interactions
2014Co-chaperonins function together with chaperonins to mediate ATP-dependent protein folding in a variety of cellular compartments. Chaperonins are evolutionarily conserved and form two distinct classes, namely, group I and group II chaperonins. GroEL and its co-chaperonin GroES form part of group I and are the archetypal members of this family of ...
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The chaperonin folding machine
Trends in Biochemical Sciences, 2002Chaperonins are versatile molecular machines that assist the folding of a wide range of substrate proteins. They harness an ATPase cycle to control access of non-native proteins to hydrophobic binding sites. ATP binding promotes large conformational changes that partially bury the hydrophobic sites and initiate the binding of a co-chaperonin, creating ...
Helen R, Saibil, Neil A, Ranson
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Chaperonin-Mediated Protein Folding
Annual Review of Biophysics and Biomolecular Structure, 2001▪ Abstract Molecular chaperones are required to assist folding of a subset of proteins in Escherichia coli. We describe a conceptual framework for understanding how the GroEL-GroES system assists misfolded proteins to reach their native states. The architecture of GroEL consists of double toroids stacked back-to-back.
D, Thirumalai, G H, Lorimer
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