10) 15 Sept 2010

10) 15 Sept 2010 - Proteins are held together by weak...

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Proteins are held together by weak interactions Loss of tertiary structure is denaturation Heat, extreme pH, organic solvents, detergents can be used to denature protein Salt increases hydrophobic affect and stabilize proteins Chaotropes destabilize tertiary structure; most useful are urea (8 M) and guanidine hydrochloride (6 M)
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Few proteins survive denaturation and renaturation Those that do are typically small compact folds like globins and ribonuclease A Ribonuclease A is a digestive enzymes that cleaves phosphodiester bonds in RNA Isolated in large quantities from bovine pancrease N H 2 NH 2 O N H 2 NH 2 NH 2 + Urea Guanidinium
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Chris Anfinson provided the first proof that a protein sequence is all that is necessary to fold a protein Renaturation – refolding to native state Dialysis is used to slowly reduce the chaotrope concentration Add urea with no reducing agent – dialyzed RNase A refolds correctly Add urea and reducing agent 1.) dialyze reducing agent then urea – RNase A is misfolded 2.) dialyze urea then reducing agent – RNase A is folded correctly
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This note was uploaded on 09/18/2011 for the course CHEM 3510 taught by Professor Mueser during the Spring '10 term at Toledo.

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10) 15 Sept 2010 - Proteins are held together by weak...

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