In article <9407080642.ZM25108 at model.phr.utexas.edu>
David G. Rhodes, rhodes at MODEL.PHR.UTEXAS.EDU writes:
>I have what may be a naive question.
>Are these discussions concerned with "real" folding (i.e. as the protein
is
>synthesized) or "experimental" folding (i.e. renaturation). There are
>parts of the discussion that suggest either possibility, and it will
make a
>big difference. ... Another way of saying that the choice of possible
>pathways is quite limited, so the distinction under discussion becomes
>somewhat less clear. (no? yes?)
If protein folding is thermodynamically controlled, then there is no
distinction between the "real" folding and "experimental" folding that
you describe.
If it does make a difference as to which amino acids come of the
ribosome first, then it is most likely kinetic control. However, this
would mean there was a different folded state for the "real" protein,
and the "experimental" protein. My opinion is this scenario
is highly unlikely.
>_____________________________________________________________________
>| David G. Rhodes | RHODES at MODEL.PHR.UTEXAS.EDU |
>| Pharmaceutics Division | |
>| College of Pharmacy | Phone:(512)471-4681 |
>| The University of Texas at Austin | Fax: (512)471-7474 }:) |
>| Austin, TX 78712-1074 | |
>|___________________________________|_______________________________|
-Ken Prehoda
kenp at nmrfam.wisc.edu
