A. Abbadi, G. Baussard, M. Marraud
Aug 1, 1986
Citations
0
Influential Citations
4
Citations
Journal
International Journal of Biological Macromolecules
Abstract
Abstract Two Boc-Asn-X-Ser-NHMe tripeptides containing a potentially N-glycosylable (X = Ala) or non-glycosylable (X = Pro) sequence have been investigated in solution by infrared and proton n.m.r. spectroscopy. In both cases, a favoured βI-folded conformation has been shown. This conformation allows a close contact between the Asn and Ser side chains by means of a Ser O γ H to Asn C γ O hydrogen bond. However, the Ala-containing tripeptide exhibits more conformational flexibility than the Pro-containing analogue, with a noticeable amount of open conformation.