Chapter9.1-Folding_and_Dynamics_truncate(2)

Chapter9.1-Folding_a - Chemistry 233 Fundamentals of Biochemistry Protein Folding 2 Molecular Chaperones Newly synthesized proteins that have not

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Chemistry 233 Fundamentals of Biochemistry Protein Folding 2
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Molecular Chaperones Newly synthesized proteins that have not folded have numerous exposed hydrophobic groups that can cause aggregation. Molecular chaperones are proteins that function to prevent or reverse these aggregations especially for multidomain and multisubunit proteins. How do they work??? They bind to these unfolded proteins’ hydrophobic surfaces, and then release them (using ATP energy in the process). They do this several times so that the protein has a chance to refold properly.
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Examples: heat shock protein 70 (Hsp70) heat shock protein 90 (Hsp90) GroEL and GroES nucleoplasmins for assembling nucleosomes (particles in which eukaryotic DNA is packaged )
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GroEL and GroES This system of chaperonin forms a large cavity in which a misfolded protein can enter and fold properly. ATP is used in the process.
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α 14 quaternary structure Shown is an electron micrograph derived image of the cavity produced by GroEL. A bound polypeptide
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This note was uploaded on 03/12/2009 for the course CHEM 233 taught by Professor Daub during the Winter '09 term at Waterloo.

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Chapter9.1-Folding_a - Chemistry 233 Fundamentals of Biochemistry Protein Folding 2 Molecular Chaperones Newly synthesized proteins that have not

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