ID #2439

Are the chaperones added to the protein in the matrix while the mitochondrial hsp70 acts as a ratchet? Also, the last slide of lecture 25 then shows the final protein going to a chaperonin. what's the point of it going to chaperonin if it already has chaperones on it? also, what is the atp used for along the arrow to the chaperonin and out of the chaperonin?

Yes, the chaperones are likely being added to the protein in the matrix as it is being ratcheted through Tim (if it needs additional folding assistance). It would make the most sense that the protein be kept unfolded until it is sent to the chaperonin, and any time that it isn't bound by chaperones the protein may fold. 
The chaperonin provides an environment that is conducive for protein folding. (Chaperonins even exclude water). The chaperones keep the polypeptide unfolded until it reaches the chaperonin. The ATP is required to open the "door" of the chaperonin to release the now-folded protein. 

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