Effect of serine O-glycosylation on cis-trans proline isomerization.

Abstract:

:In order to examine the ability of an O-glycosylated serine residue preceding proline to stabilize a cis amide conformation in a fashion similar to that observed with aromatic amino acid residues, we prepared a series of glycosylated analogs of a small linear peptide which we have previous reported to contain a cis conformation of an amide bond between tyrosine and proline. The glycopeptides were prepared by incorporating glycosylated N alpha- (fluoren-9-yl) methoxycarbonyl (Fmoc) amino acids into a standard solid phase peptide synthesis protocol. The peptides and glycopeptides were analyzed using 2-dimensional NMR spectroscopy. Unlike the case where the residue preceding proline was tyrosine, no signals corresponding to a cis proline conformation were detected in the spectra of the two glycopeptides containing serine O-glycosylated with either beta-linked N-acetyl glucosamine or alpha-linked N-acetyl galactosamine in the position preceding proline.

authors

Pao YL,Wormarld MR,Dwek RA,Lellouch AC

doi

10.1006/bbrc.1996.0198

subject

Has Abstract

pub_date

1996-02-06 00:00:00

pages

157-62

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)90198-9

journal_volume

219

pub_type

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