lec 25 - Lecture 25 Protein folding modification and...

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Lecture 25: Protein folding, modification and degradation
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From Alberts et all, Mol Biol of the Cell, 4th ed. Protein folding ! Protein is usually divided in “folding units” = domains!
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denaturation (urea) denaturation (urea) renaturation renaturation native (“right”) conformation wrong conformation aggregation CHAPERONES Protein folding: in vitro conversion between native and denatured conformations insoluble What happens to misfolded proteins?
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Chaperones/chaperonins help protein folding Chaperones bind to exposed hydrophobic residues of nascent polypeptide, help folding, and protects from aggregation until properly folded
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Chaperones/chaperonins help protein folding =Hsp60 Chaperonins recognize hydrophobic surfaces of proteins (thus misfolded), unfold the protein and allows refolding in a “protected” environment (partially hydrophobic cavity).
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Chaperones/chaperonins help protein folding =Hsp60 Question: What are the similarities in hsp60 and Hsp70?
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Post-transcriptional modifications: covalent modifications protects N-terminus from attack by exopeptidases end of polypeptide, free NH2
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