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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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CHAPERONIN FUNCTION DEPENDS ON STRUCTURE AND DISORDER IN CO-CHAPERONIN MOBILE LOOPS
Biocomputing '99, 1998Co-chaperonins from diverse organisms exhibit mobile loops which fold into a beta hairpin conformation upon binding to the chaperonin. GroES, Gp31, and human Hsp10 mobile loops exhibit a preference for the beta hairpin conformation in the free co-chaperonins, and the conformational dynamics of the human Hsp10 mobile loop appear to be restricted by ...
S. J. Landry +4 more
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Effect of bacteriophage-encoded chaperonins on amyloid transformation of α-synuclein
Biochemical and Biophysical Research Communications, 2022Sofia S Kudryavtseva +2 more
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Chaperonins in cancer: Expression, function, and migration in extracellular vesicles
Seminars in Cancer Biology, 2022Everly Conway de Macario +1 more
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Chaperonins in Health and Disease
Annals of the New York Academy of Sciences, 1998A R, Coates, B, Henderson
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