3.Protein_folding

3.Protein_folding - Protein Folding Protein Folding The...

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Protein Folding
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Protein Folding The process by which a protein goes from  being an unfolded polymer with no activity to a  uniquely structured and active protein
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Why do we care about protein folding? If we understand how proteins fold, maybe it  will help us predict their three-dimensional  structure from sequence information alone or  even design our own proteins Protein misfolding has been implicated in  many human diseases (Alzheimer’s,  Parkinson’s, . ..)
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Protein folding in vitro is often reversible Chris Anfinsen - 1957 1. Reduction with HOCH 2 CH 2 SH 2. Denature with 8M urea 1. Remove Urea and renature 2. Oxidize
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The probability for correctly forming 4 disulfide bonds is  1% 1 7 x 1 5 1 3 1 1 x x = 1 105 = ~1%
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Protein folding in vitro is often reversible Chris Anfinsen - 1957 1. Reduction with HOCH 2 CH 2 SH 2. Denature with 8M urea 1. Oxidize 2. Remove Urea and renature “scrambled” RNase A only 1% active Proteins self-assemble spontaneously directed by primary structure
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Observations that have affected our view of protein  folding 1. -helices and   pleated sheets fill space  α β efficiently Simulations show helix and sheet-like structures  form spontaneously from flexible chains to fill  space 1. Mutations to internal residues are much more  likely change a protein’s conformation Burying hydrophobic residues drives protein folding
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Observations that have affected our view of protein  folding 1. Protein structures are hierarchically organized
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How do proteins fold? Do proteins fold by performing an exhaustive 
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3.Protein_folding - Protein Folding Protein Folding The...

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