| Description |
1 online resource (1 streaming video file (30 min.) : color, sound) |
| Series |
Protein homeostasis : folding proteins and maintaining the protein-protein interaction networks, 2056-452X |
|
Henry Stewart talks. Biomedical & life sciences collection. Protein homeostasis
|
| Contents |
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 |
| Notes |
Animated audio-visual presentation with synchronized narration |
|
Title from title frames |
|
Mode of access: World Wide Web |
|
System requirements: Browser compatibility: updated Mozilla Firefox, Google Chrome, Safari or Internet Explorer 8+. Browser settings: enable JavaScript, enable cookies from the Henry Stewart Talks site. Required Desktop Browser plugins & viewers: Updated Adobe Flash Player & Adobe Acrobat Reader. Mobile device & operating system versions: Android v4.0+, iPhone 4+ (iOS v6.x+), iPad 2+ (iOS v6.x+), BlackBerry OS v7.0+, Windows Phone v6.5.1+ |
| Subject |
Molecular chaperones.
|
|
Protein folding.
|
|
Chaperonin 10 -- metabolism.
|
|
Chaperonin 60 -- metabolism.
|
|
Chaperonins -- metabolism.
|
|
Molecular Chaperones.
|
|
Protein Folding.
|
| Genre/Form |
Video recordings.
|
| Form |
Streaming video
|
|
