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Outline - Chapter 6 - -Activation of a ubiquitin ligase e.g...

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Chapter 6 Protein folding, degradation, and misfolding (pages 387-398; figures 6-82 to 6-96) 1. Some proteins begin to fold while being synthesized - co-translational protein folding 2. Molecular chaperones help protein folding - heat-shock proteins (hsp) - hsp 60 and hsp 70 molecular chaperones share affinity for exposed hydrophobic patches 3. Proteasome - processive protein degradation 4. Ubiquitin conjugating system marks proteins for destruction 5. Many proteins are controlled by regulated destruction
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Unformatted text preview: -Activation of a ubiquitin ligase e.g. APC by addition of a subunit-Signals create a degradation signal in the target protein e.g. N-end rule-In yeast – 12 destabilizing residues-Arg, lys, his, phe, leu, tyr, trp, ile, asp, glu, asn, gln 6. Abnormally folded proteins form aggregates-Resistant to proteolysis-Cross-beta filament-Prion diseases – CJD in humans, BSE in cattle-“Protein-only inheritance”...
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