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Protein Science, Vol 6, Issue 3 637-648, Copyright © 1997 by Cold Spring Harbor Laboratory Press

ARTICLE

Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides

A. A. VAN-DIJK, L. L. VAN-WIJK, A. VAN-VLIET, P. HARIS, E. VAN-SWIETEN, G. I. TESSER and G. T. ROBILLARD
Department of Biochemistry and Biophysical Chemistry and the Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands Present address: Gist Brocades N.V. Postbus 1, 2600 MA, Delft, The Netherlands.

The high molecular weight (HMW) proteins from wheat contain a repetitive domain that forms 60-80% of their sequence. The consensus peptides PGQGQQ and GYYPTSPQQ form more than 90% of the domain; both are predicted to adopt {beta}-turn structure. This paper describes the structural characterization of these consensus peptides and forms the basis for the structural characterization of the repetitive HMW domain, described in the companion paper. The cyclic peptides cyclo-[PGQGQQPGQGQQ] (peptide 1), cyclo-[GYYPTSPQQGA] (peptide 2), and cyclo-[PGQGQQGYYPTSPQQ] (peptide 3) were prepared using a novel synthesis route. In addition, the linear peptides (PGQGQQ)(n) (n = 1, 3, 5) were prepared. CD, FTIR, and NMR data demonstrated a type II {beta}-turn structure at QPGQ in the cyclic peptide 1 that was also observed in the linear peptides (PGQGQQ)(n). A type I {beta}-turn was observed at YPTS and SPQQ in peptides 2 and 3, with additional {beta}-turns of either type I or II at GAGY (peptide 2) and QQGY (peptide 3). The proline in YPTS showed considerable cis/trans isomerization, with up to 50% of the population in the cis-conformation; the other prolines were more than 90% in the trans conformation. The conversion from trans to cis destroys the type I {beta}-turn at YPTS, but leads to an increase in turn character at SPQQ and GAGY (peptide 2) or QQGY (peptide 3).
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