Hi
If anyone could give me a short hint:
I thought of synthesizing some small peptides (10-25 mers) to produce antibodies against an
enzyme of which the gene (and protein-) sequence is known (instead of isolating the protein and
using it for an immunisation). The crucial point is, as I believe, to select regions from the
protein structure that are on the 'outside' of the folded protein and thus accessible to
antibody binding.
Is there a way to determine or predict which part of a protein sequence is likely to appear on
the 'outside' of the folded protein (a rough algorithm based estimation e.g.)?
Or do I simply have to select hydrophilic regions of the sequence (it's a periphal membrane
protein when active - probably attached to the membrane by another protein - and found in the
cytosol when inactive) because they are likely to be neccesary for keeping the enzyme in
solution.
Is there a better chance to be successful if selecting a region near the N- or the C-terminus
or in the middle?
Should I avoid selecting regions that are known or supposed to be binding sites for other
proteins or domains for substrates?
I already have been conducting a medline research but did'nt find anything appropriate yet
(protein and (synthe* or design) and (antibod* and production), so I'm now posting to this
newsgroup.
What do you think? I appreciate ANY comment. Maybe you know a good book or journal article or
have experince of your own. Please mail, too.
Thanks a lot in advance!
+++++++++++++++++++++++++++++++++++++++
Wolfgang Schechinger
Institute for Diabetes Research
Koelner Platz 1
80804 Munich
Germany
Phone + 49 (89) 30 79 31 24
Fax + 49 (89) 30 81 733
email u7k0201 at sunmail.lrz-muenchen.de
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