5 - Tail-to-tail heptamers Cage for folding GroEL/GroES...

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Fig. 3-21 Lehn
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Fig. 3-21 Lehn
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Lehn. 3-21
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Fig. 4-26 Lehn
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Fig. 4-26 Lehn
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Fig. 4-27 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. 4-28 Lehn
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Lehn. Fig. 2-7 (b)
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Fig. 6-7 B and T
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Fig. 6-7 B and T
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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 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)- Found universally – prokaryotes and eukaryotes
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Unformatted text preview: Tail-to-tail heptamers Cage for folding GroEL/GroES (Hsp60/Hsp10) Fig. 4-30 Lehn GroEL (Hsp60) Fig. 4-31 Lehn Fig. 4-30 Lehn Amyloidoses Diseases where mutant forms of normally occurring proteins accumulate in tissues as AMYLOID (insoluble aggregates) 2 very different stable protein conformations Native form Amyloid form Taylor et al. Science 296:1991(02) Alzheimers Picks (tau) Prion Parkinsons (Lewy) Taylor et al. Science 296:1991(02) -cross Fibers: helical arrangement of -strands perpendicular to the fiber axis Protein fibrils rich in -sheets, even though native state of the proteins may lack -sheets Large number of fibrils adopt -cross conformation Taylor et al. Science 296:1991(0 tanley Prusiner Nobel Prize 997 RIONS Protein Structure and Function in the Immune System...
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5 - Tail-to-tail heptamers Cage for folding GroEL/GroES...

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