2011_10_05_protein_folding2

2011_10_05_protein_f - Protein Folding in the Cell in vivo protein fold efficiently into native conformation as they are being synthesized(~sec to

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Protein Folding in the Cell - in vivo protein fold efficiently into native conformation as they are being synthesized (~sec to min) - cells contain 3 types of accessory proteins to assist folding: 1) Protein disulfide isomerases (PDIs) - catalyzes disulfide interchange 2) Peptidyl prolyl cis-trans isomerases (PPIs) - catalyzes the slow interconversion of X-Pro peptide bonds between cis and trans 3) Molecular chaperones - prevent or reverse aggregation by binding to an unfolded chain’s solvent exposed hydrophobic regions and releasing them, repeatedly, in an ATP dependent manner (ATPases) - Hsp70, Hsp90, chaperonins (GroEL/ES)
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GroEL/GroES chaperonin
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Protein Dynamics Proteins are flexible due to marginal stability (i.e. not very negative Δ G) with functionally important structural motions eg. hemoglobin cooperativity Intramolecular motions of proteins can be classified into 3 categories: 1) atomic fluctuations - vibrations of individual bonds (10 -15 to 10 -11 sec) - spatial displacement 0.01 to 1 Å
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This note was uploaded on 10/21/2011 for the course BIOC 450 and 45 taught by Professor Various during the Fall '11 term at McGill.

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2011_10_05_protein_f - Protein Folding in the Cell in vivo protein fold efficiently into native conformation as they are being synthesized(~sec to

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