November
2001
Volume
78
Number
6
Pages
658
—
662
Authors
O.
Parchment
,
1
P. R.
Shewry
,
2
,
3
A. S.
Tatham
,
2
and
D. J.
Osguthorpe
1
Affiliations
Molecular Graphics Unit, School of Chemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK.
IACR-Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol BS41 9AF, UK.
Corresponding author. Phone +44 (0) 1275 549330. Fax: +44 (0) 1275 394281. E-mail: arthur.tatham@bbsrc.ac.uk
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RelatedArticle
Accepted July 2, 2001.
Abstract
ABSTRACT
The structure of the central repetitive domain of the high molecular weight glutenin subunits, a group of elastomeric proteins from the seeds of wheat, were modeled using structure prediction and molecular dynamics. Models were generated with spiral structures, based on repetitive β-reverse turns, within and spanning the repeat motifs of the central domains. The models were consistent with available data from biophysical studies on the intact proteins and spectroscopic (infra-red and nuclear magnetic resonance) studies of synthetic peptides.
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ArticleCopyright
© 2001 American Association of Cereal Chemists, Inc.