"Artem Evdokimov" <AEVDOKIMOZ at cinci.rr.com> schrieb:
> Cutting/adding/mutating residues at the termini is VERY OFTEN bad for the
> folding. Keep in mind that oftentimes having extra residues is bad
> too.
I would have argued that this is rather a question of solubility,
i.e. "sticky ends" of a protein aggregate? Can you give some examples?
> In
> my field (crystallography) frequently the nature of the game is to find the
> minimal-and-sufficient domain (or truncated protein) which will fold
> correctly. It all depends on how much you cut - obviously if you remove a
> residue that's crucial for folding your protein will not work out. We
> routinely screen termini truncations for efficient folding and
> crystallization.
Hm. If you don't cut enough, you get loose termini, which don't
interfere with folding (because this is the near-native sequence), but
inhibit crystallization. If you cut too much, you get a problem because
you cut beyond the "terminus" and deleted a residue that is in the bulk
of the structure. That's how I see it..
Bye, Frank
