QUESTIONS: alpha-helix "signals" in proteins

Ken Prehoda kenp at nmrfam.wisc.edu
Fri Jul 8 09:00:27 EST 1994

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
>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

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