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UCSD BIBC 100 - Folding

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The sequence that you used the BLASTalgorithm to identify is a:A.Rodent preproinsulinB.Human insulinC.Chimp insulinD.Human preproinsulinE.I didn’t do the exercise yet.Fig. 4-27 LehnFig. 4-27 LehnFig. 4-28 LehnFig. 6-2 B and TMolten Globule Final folded formFig. 6-5B and TFig. 4-29LehnCrowded cytoplasm(tRNA in blue, ribosomes in green,proteins in red)Molecular Chaperones function analogously to human counterparts:“They inhibit inappropriate interactions between potentially complementary surfaces and disrupt unsuitable liasons so as to facilitate more favorable associations”John EllisGeneral Features ofChaperones• Proteins that catalyze the folding of other proteins– Folding information in primary sequence of proteins– But, cellular concentration of proteins ~300 mg/ml– Aggregation– Rate of chain elongation is ~ 4 amino acids/second, soabout ~ 4 minutes for a 1000 residue protein– Exposed hydrophobics• Initially identified as proteins induced by heat shock —heat shock proteins (Hsp)Peptide prolyl cis-trans isomerase (PPI)catalyzes this reactionProtein disulfide isomerase (PDI) can greatly speed up this reactionGiven the enzymatic activity of a PDI(protein disulfide isomerase, where doyou expect most of this enzyme to befound in a eukaryotic cell?A.NucleusB.CytosolC.Endoplasmic reticulumD.Cell surfaceE.On or near


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UCSD BIBC 100 - Folding

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