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Lect5folding - – But cellular concentration of proteins...

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The sequence that you used the BLAST algorithm to identify is a: A.Rodent preproinsulin B.Human insulin C.Chimp insulin D.Human preproinsulin E.I didn’t do the exercise yet.
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Fig. 4-27 Lehn
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Fig. 4-27 Lehn
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Fig. 4-28 Lehn
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Fig. 6-2 B and T
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Molten Globule Final folded form
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Fig. 6-5 B and T
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Fig. 4-29 Lehn
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Crowded cytoplasm (tRNA in blue, ribosomes in green, proteins in red)
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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 Ellis
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General Features of Chaperones Proteins that catalyze the folding of other proteins Folding information in primary sequence of proteins
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Unformatted text preview: – But, cellular concentration of proteins ~300 mg/ml – Aggregation – Rate of chain elongation is ~ 4 amino acids/second, so about ~ 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 reaction Protein disulfide isomerase (PDI) can greatly speed up this reaction Given the enzymatic activity of a PDI (protein disulfide isomerase, where do you expect most of this enzyme to be found in a eukaryotic cell? A.Nucleus B.Cytosol C.Endoplasmic reticulum D.Cell surface E.On or near Ribosomes...
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