Can someone tell me what evidence exists as to what exactly
the heat shock proteins(hsp) do in helping proteins fold.
My question specifically is this:
A partially folded species binds the chaperone. Then after a
time it comes out. Is there any evidence that the form that comes out
is actually a native structure? Is it possible that the molecule that
comes out is just the same as the one that went in?
If infact the protein comes out fully folded, it stands to reason
that the hsp actually brings different parts of the partially
folded species together. This would seem to indicate the need for
relatively large changes in conformation for the hsp. Is there any
evidence that this really occurs? Some hsp's use ATP. So apriori there
is no reason toreject the `mechanistic view' that they `pull'
the protein together. But I would like to know if there is any evidence
that this really occurs.
Thanks in anticipation.
Kamalakar Gulukota
