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Inside the chaperonin toolbox: theoretical and computational models for chaperonin mechanism
Physical Biology, 2009Despite their immense importance to cellular function, the precise mechanism by which chaperonins aid in the folding of other proteins remains unknown. Experimental evidence seems to imply that there is some diversity in how chaperonins interact with their substrates and this has led to a number of different models for chaperonin mechanism ...
Del, Lucent +2 more
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On the oligomeric state of chloroplast chaperonin 10 and chaperonin 20
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003Type I chaperonins are fundamental protein folding machineries that function in eubacteria, mitochondria and chloroplasts. Eubacteria and mitochondria contain chaperonin systems comprised of homo-oligomeric chaperonin 60 tetradecamers and co-chaperonin 10 heptamers.
Rajach, Sharkia +7 more
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Protein folding and chaperonins
Plant Molecular Biology, 1992The folding of polypeptide chains in cells, following either translation or translocation through membranes, must take place under conditions of extremely high protein concentrations. In addition, folding into a correct structure must occur in the presence of other rapidly folding species, and at temperatures known to destabilize aggregation-prone ...
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Mammalian cytosolic chaperonin.
Methods in enzymology, 1998Cytosolic chaperonin, the eukaryotic cytosolic homolog of GroEL, has certain unusual features that make it uniquely useful for studying the mechanism of chaperonin action. It is of particular interest as an essential component in the generation of native actin and tubulin in vivo. We describe a method for the purification of mammalian c-cpn from rabbit
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