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dc.contributor.authorBeyreuther, Konrad
dc.contributor.authorSchulze-Gahmen, Ursula
dc.contributor.authorBieseler, Barbara
dc.contributor.authorPrinz, Heinrich
dc.date.accessioned2023-04-26T09:46:00Z
dc.date.available2023-04-26T09:46:00Z
dc.date.issued1987
dc.date.submitted2023-04-26
dc.identifier.citationChemical synthesis in molecular biology, 199 ffen_US
dc.identifier.issn0930-4320
dc.identifier.urihttp://hdl.handle.net/10033/623371
dc.description.abstractWe performed model studies towards assignment of &-turn and a-helices to protein primary structures with antibodies. Probing of a &-turn was attempted with anti-peptide antibodies directed against the &-turn (DPGQ) of a synthetic &-turn model-peptide (IVIVIDPGQTVTY) adopting the intended conformation &-sheet-&-turn-&-sheet. The specific anti-&-turn model-peptide antibodies have a three orders of magnitude higher affinity for the &-turn containing epitope than the control Gly-peptide (GsDPGQG,, ) of random coil structure. The antibody affinity for the &-turn region (DPGQ) increases from the primary to the hyperimmune response. Although the chosen &-turn sequence is similar to parts of the animal's own proteins, self-tolerance did not raise difficulties in generating antibodies against the R-turn model-peptide. Individual putative &-turn sequences of proteins may be probed by including their sequence between the two &-sheet cartridges of the &-turn model-peptide. Helix assignment was probed with synthetic model peptides of extended conformation including only the superimposed residues of a putative helix (every fourth residue) linked by a spacer amino acid residue (alanine throughout or the corresponding third residue of the sequence to be tested) in order to adjust the translation of the relevant residues of the model-peptide to the helical pitch. The anti-helix modelpeptide antibodies were shown by Western blotting to react in a sequence-specific manner with the corresponding model protein lactose permease of E.coli. "Conformational sequencing" i.e. sequence assignments of secondary structures by anti-peptide antibodies now seems feasable for &-turn regions and helices of proteins of known sequence.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesGBF Monographs, Vol. 8en_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleTOWARDS CONFORMATIONAL SEQUENCING OF PROTEINS: ASSIGNMENT OF SECONDARY STRUCTURES BY ANTI-PEPTIDE ANTIBODIESen_US
dc.typeBook chapteren_US
dc.typeconference paperen_US
dc.contributor.departmentInstitute for Genetics, University of Cologne Weyertal 121, D-5000 Cologne 41, F.R. Germanyen_US
dc.identifier.journalChemical synthesis in molecular biologyen_US
refterms.dateFOA2023-04-26T09:46:00Z


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Attribution-NonCommercial-ShareAlike 4.0 International
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