Outline - Chapter 6 - Chapter 6 Protein folding,...

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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 - To be an active protein, the polypeptide mst foldi into the correct conformation, bind cofactors, be modifided by kinases and other proteins and assemble all subunits. - Hydrophobic interactions and non covalent bonds help get polypeptides in the confromation of lowest energy. This has been selected for via evolution. - Synthesis begins at the N-terminus and most alpha and beta secondary structures are formed soon after production. This is called co-ranslational protein folding. 2. Molecular chaperones help protein folding - Molecular chaperones help proteins fold into the right shape. They include heat shock proteins (Hsp’s)which are synthesized dramatically after cells are exposed to high temperatures to help refold misfolded proteins. - Hsp60 and Hsp7 are families of eukaryotic chaperones. Mitochondria and the cytosol have their own versions of each of these proteins. BIP is a special version of Hsp70 in the ER. - Hsp’s and chaperones have an affinity for exposed hydrophobic regions on incompletely folded
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This note was uploaded on 03/24/2011 for the course BIO 320 taught by Professor Staff during the Spring '08 term at University of Texas at Austin.

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Outline - Chapter 6 - Chapter 6 Protein folding,...

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