Ontology type: schema:ScholarlyArticle
1997-12
AUTHORSAlain Bac, Katell Rivoal, Manh Thong Cung, Guy Boussard, Michel Marraud, Benoît Soudan, Daniel Tetaert, Pierre Degand
ABSTRACTConsequences inherent to the substitution of aza-proline (AzPro) for proline in the octapeptide TTSAPTTS, representative of the tandem repeat motif present in the peptide backbone of MUC5AC mucin, were analysed in terms of conformational perturbation and O-glycosylation aptitude. In DMSO solution, we observed the same tendency previously noted in AzPro-tripeptide models, i.e. AzPro prevents β-turn formation in which it would occupy the i+1 position, and therefore behaves quite opposite to Pro, whereas both AzPro and Pro can support a β-turn in the i+2 position with a cis disposition of the preceding tertiary amide function. The former structural modifications do not prevent O-glycosylation to take place at the same specific site, but it occurs at a reduced rate. More... »
PAGES251-258
http://scigraph.springernature.com/pub.10.1007/bf02442885
DOIhttp://dx.doi.org/10.1007/bf02442885
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