当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Synthesis and conformational analysis of Aib-containing peptide modelling for N-glycosylation site in N-glycoprotein.

Synthesis and conformational analysis of Aib-containing peptide modelling for N-glycosylation site in N-glycoprotein.

Abstract：

:A tetrapetide containing an Aib residue, Boc-Asn-Aib-Thr-Aib-OMe, was synthesized as a peptide model for the N-glycosylation site in N-glycoproteins. Backbone conformation of the peptide and possible intramolecular interaction between the Asn and Thr side chains were elucidated by means of n.m.r. spectroscopy. Temperature dependence of NH proton chemical shift and NOE experiments showed that Boc-Asn-Aib-Thr-Aib-OMe has a tendency to form a beta-turn structure with a hydrogen bond involving Thr and Aib4 NH groups. Incorporation of Aib residues in the peptide model promotes folding of the peptide backbone. With folded backbone conformation, carboxyamide protons of the Asn residue are not involved in hydrogen bond network, while the OH group of the Thr residue is a candidate for a hydrogen bond in DMSO-d6 solution.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Ishii H,Nadaoka O,Mimura Y,Inoue Y,Chûjô R

doi

10.1016/0141-8130(89)90003-2

subject

Has Abstract

pub_date

1989-12-01 00:00:00

pages

329-34

issue

6

eissn

0141-8130

issn

1879-0003

pii

0141-8130(89)90003-2

journal_volume

11

pub_type

杂志文章

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