Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
Article Abstract:
Research has been conducted on the TRP domains of the adaptor protein Hop. Results indicate that TRP domains participate in the Hsp70-Hsp90 maltichaperone complex ordered assembly.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
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Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil trentacles with unfolded proteins
Article Abstract:
Research elucidates the molecular structure of prefoldin hexamer from the archaeum Methanobacterium thermoautotrophicum. Data show that the chaperone protein structure exhibits a jellyfish-like appearance with double beta barrel assembly and six long protruding tentacle-like coils.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
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Dual function of protein confinement in chaperonin-assisted protein folding
Article Abstract:
Research shows that the cage formed by the GroEL protein coupled with its cofactor GroES, which together form a chaperonin system, exhibits a dual role in promoting protein folding.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2001
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