Conformational aspects of Boc-Phe-Pro-Asn-Ala-Thr-NHMe; A model of a N-glycosylation site in ovomucoid.
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概要
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A peptide sequence (Boc–Phe–Pro–Asn–Ala–Thr–NHMe) corresponding to one of the <I>N</I>-glycosylation sites in hen egg ovomucoid was studied with its related fragment analogues, Boc–Pro–Asn–Ala–Thr–NHMe, Boc–Asn–Ala–Thr–NHMe, and Boc–Ala–Thr–NHMe by NMR and CD to investigate their backbone conformations and possible intramolecular interactions. From the CD study, Boc–Phe–Pro–Asn–Ala–Thr–NHMe may adopt some ordered structures in aqueous solution. However, in this peptide series, there is no stable hydrogen bonds involving backbone amide protons nor is there any definitive evidence for intramolecular hydrogen bonds involving Asn and Thr side chains. But, it is evident from the temperature study of chemical shifts that the hydrogen bonding tendency of the Thr hydroxyl protons and the Asn carboxyamide protons is dependent on both the triplet sequence and chain length of the peptide analogues. The potential to form some kind of loop structure rather than the presence of some stable secondary structure is indicated.
- 社団法人 高分子学会の論文
社団法人 高分子学会 | 論文
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