Aggregation of proteins on refolding
kgg6519 at uxa.cso.uiuc.edu
Mon Aug 31 09:42:36 EST 1992
Here is a question on Protein refolding experiments. Can someone
please answer it.
Many proteins on refolding give only partial activity because the
rest of the protein has aggregated. It is supposed that it is really
some partially folded intermediates on the folding pathway that form
interactions with other molecules rather than have intramolecular
interactions to form the native structure. How much of the protein
(what %) aggregates depends upon the nature of the protein as well as,
in some cases, on the method of refolding (or, perhaps more to the point,
the method in which the protein was denatured in the first place). Now,
the question is this: Does it make sense to talk about a single number
as the percentage of the protein that aggregates? i.e. is there a limit
that aggregation reaches? If I found 30% aggregation at 2 hours, would
I find 35% at 3 hours and so on? If I waited long enough, would aggregation
in any protein refolding process reach 100%?
Undoubtedly, the RATE of aggregation decreases with time. But does
it ever get close enough to zero that we can say that the aggregation
at that time is the limit and that at time = infinity, the % aggregation
would still be about the same?
Thanks very much in advance
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