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.

Peptides, Cell research, Cytological research

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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.

Heat shock proteins, Crystals, Crystal structure, Stability

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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.

Escherichia coli, Protein folding, Structure-activity relationships (Biochemistry)

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