ffrank at rz.uni-potsdam.de (Frank Küster geb. Fürst) wrote,
that's me:
> "Artem Evdokimov" <AEVDOKIMOZ at cinci.rr.com> schrieb:
>> > > You're right. Things are always more complicated if you look closer. One
> > > other example, kind of extreme, comes to my mind: Pro-domain assisted
> > > folding, e.g. in alpha-lytic protease, which is less stable than the
> > > unfolded form after the pro-domain has been cleaved.
> >
> > Let's not forget concanavalin A which is expressed as a chain that undergoes
> > cleavage and re-ligation with a large piece turned around :)
>> Is it turned around? I never had close look at the sequence or the
^^ a close look...
> strucutre. But in the legume lectin reviews I read (and I read a couple
> in the last months), they always say that it is circularly
> permuted. That would mean that there is no change in the structure, only
> the old termini are re-ligated and the new ones are free. The original
> termini are very close to each other in the legume lectin monomer
> (separated just by a "non-existing" beta-turn).
I wanted to say: The termini are located relative to each other in a way
that permits to easily connect them by a beta-turn (and this what is
done in ConA, I think). They are oriented correctly, only the connecting
bond is missing.
> I think nobody knows which effect this procedure has on ConA folding,
> because it folds first, and I am not aware of any in vitro study on ConA
^^^^^
before it is processed. At least this is the case for the other
processed legume lectins, pea and lentil lectins and the /vicia/
lectins, which are only cut (elsewhere) and not re-ligated.
Bye, Frank
--
sigmentation fault
