The interaction network of the GroEL chaperonin [electronic resource] / F. Ulrich Hartl.
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FilmSeries: Henry Stewart talksBiomedical & life sciences collection. Protein homeostasis: Publisher: London : Henry Stewart Talks, 2012Description: 1 online resource (1 streaming video file (30 min.) : color, sound)Subject(s): Molecular chaperones | Protein folding | Chaperonin 10 -- metabolism | Chaperonin 60 -- metabolism | Chaperonins -- metabolism | Molecular Chaperones | Protein FoldingOnline resources: Click here to access online | Series Animated audio-visual presentation with synchronized narration.
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Contents: De novo protein folding and proteome maintenance critically depend on molecular chaperones -- Transitions during protein folding -- Chaperone assisted protein folding -- Productive protein folding is often competed by aggregation -- Reconstitution of GroEL-assisted folding -- GroEL and GroES function as a folding cage for proteins up to 60 kDa -- GroEL structure -- Which proteins need GroEL/GroES for folding? -- Identification of the GroEL interaction proteome -- Class III substrates are of relatively low cellular abundance but occupy most of the GroEL capacity -- Chaperonins provide a specialized folding environment with two functional elements: sequestration and steric confinement in a hydrophilic cage -- GroEL as part of the cytosolic chaperone network.
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Mode of access: World Wide Web.