Lectures 6 & 7 - Proteinfolding and Chaperones

Lectures 6 & 7 - Proteinfolding and Chaperones -...

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Protein folding & Chaperones
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Characteristics of Folded State Tight packing – compact Sequence determined/environment modulated Families and symmetry Each sequence unique structure Native state is thermodynamically stable Lowest energy
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Physics of Folding Enthalpy drives towards this HB interactions – H bonding – Ionic interactions Free Energy is the Difference Folded state is more stable Entropy drives towards this HB exposed
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Steps of Folding Unfolded bury core 2 o Molten globule 3 o 4 o protein HB aa (loose 3 o ) (breathing) < ms Up to 1s
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Why won’t it fold? Most common obstacles to a native fold: Aggregation Non-native disulfide bridge formation Isomerization of proline
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Energy Funnel for Folding Multiple folding pathways can occur Model this with energy funnel
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Chaperonins / Heat Shock Proteins HSPs help proteins fold by preventing aggregation Recognize only unfolded proteins Not specific
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Lectures 6 &amp;amp; 7 - Proteinfolding and Chaperones -...

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