Lord of the rings: GroES structure
Article Abstract:
Protein folding in Escherichia coli popypeptide synthesis requires the chaperonins GroEL and GroES. Two studies of GroES structure have aided understanding of the mechanism of GroEL-GroES interaction. Results of the studies are discussed.
Publication Name: Science
Subject: Science and technology
ISSN: 0036-8075
Year: 1996
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From the cradle to the grave: ring complexes in the life of a protein
Article Abstract:
Both the chaperonin GroEL, which plays a role in protein folding, and proteasome, which promotes protein degradation, have very similar cylindrical ring structures. Details of their architecture and functions are discussed.
Publication Name: Science
Subject: Science and technology
ISSN: 0036-8075
Year: 1995
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To fold or not to fold...
Article Abstract:
The molecular chaperone Hsp70 is one mechanism that cells use to prevent protein aggregation. The process by which Hsp binds to unfolded and partially folded proteins is described.
Publication Name: Science
Subject: Science and technology
ISSN: 0036-8075
Year: 1993
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