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Lectures 6 7 - Proteinfolding and Chaperones

Not specific recognizes exposed hb patches prevent

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– Not specific – Recognizes exposed HB patches – Prevent aggregation of unfolded or misfolded proteins • HSP70 – Regulate translocation to ER – Work as a complex
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• Each subunit –A p i c a l (  motif) • Opening of chaperone to unfolded protein •F le x ib le •HB – Intermediate ( helices) • Allow ATP and ADP diffusion
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• Cap to the GroEL • Each subunit sheet hairpin (roof) – Mobile loop (int w/ GroEL) • 7 subunits in functional molecule GroES
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GroEL+ GroES work together • GroEL makes up a cylinder – Each side has 7 identical subunits – Each side can accommodate one unfolded protein • 1 GroES binds to one side of GroEL at a time – Allosteric inhibition at other site • One side of cylinder is actively folding protein at a time
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1.GroEL/ATP complex at side A 2.Bind GroES on this side 7 ATP 7 ADP this side has a wider cavity but closed top other side has smaller cavity and open top 3.Side B ring binds unfolded protein GroES falls off of side A ADP falls off of side A 4.Side B ring binds 7 ATPs 5.GroES binds GroEL/ATP 7 ATP 7 ADP protein folding occurs 6.Side A ring binds 7 ATPs protein folding occurs 7 ATP 7 ADP (side A) 7.Side A ring binds next unfolded protein
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• Switch side of ATP binding each time • Switch side of GroES binding for each folding rxn • Switch side of protein docking for each folding rxn Fink, Chaperone Mediated Folding, Physiological Reviews, 1999 Mechanism of Chaperonin Function
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