cis/trans Proline
moreaut at univ-tours.fr
moreaut at univ-tours.fr
Mon Nov 28 12:55:07 EST 1994
dear netters,
I have a peptide substrate, the sequence of which is
Ala-Gly-Pro-Arg-Ser-Leu
This peptide and a second one 4 residues longer at the N-ter side have
been synthezised in order to study the specificity of a serine proteinase.
The longest peptide is rapidly cleaved at the Arg/Ser bond as expected
but the efficiency of cleavage (i.e the kcat/Km ratio) is reduced for
the short peptide. My questions are:
1/ which conformation of the Pro residue can we expect for such a short
peptide i.e cis, trans or do both forms equilibrate?
I know that cis forms of Pro sometimes occur in proteins but I do not
know what happens for short peptides.
2/ if we have 80% of cis form in the short peptide, should we still have
80% of cis form in the long peptide?
3/ is it possible that one form (i.e cis or trans) could be a better
substrate than the other one for the protease?
Thanks in advance for your help and for any comments
*------------------------------------------------------------------*
| Dr. Thierry MOREAU |
| |
| Laboratoire d'Enzymologie et Chimie des Proteines |
| |
| URA CNRS 1334 Phone: (33) 46 36 62 06 |
| 2bis, Bd Tonnelle Fax: (33) 47 36 60 46 |
| 37032 TOURS cedex Email: moreaut at univ-tours.fr |
| FRANCE |
| |
*------------------------------------------------------------------*
More information about the Proteins
mailing list