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In cells, folding of the protein tau is typically assisted by chaperoneswhich themselves change shape during the folding of the targetedprotein. Describe how the shape changes in two different types of chaperones - Hsp70 and Hsp60 - are coupled to folding of newly synthesized tau and the role of ATP in this process. Improperly folded tau is targeted for destruction, but the native (properly folded) tau is not. Explain the reason for the different fates of these two versions of the tau polypeptide. Some folded forms of tau accumulate and cause serious neurological disease called “tauopathies”; what might account for this aberrant tau accumulation?

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Sixta Kovacek
Sixta KovacekLv2
29 Sep 2019

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