Molecular structures and interactions of repetitive peptides based on wheat glutenin subunits depend on chain length

Feeney, K. A., Wellner, N., Gilbert, S. M., Halford, N. G., Tatham, A. S., Shewry, P. R. and Belton, Peter (2003) Molecular structures and interactions of repetitive peptides based on wheat glutenin subunits depend on chain length. Biopolymers, 72 (2). pp. 123-131. ISSN 0006-3525

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Abstract

Synthetic and recombinant peptide models of the central repetitive domain of the high molecular weight subunits of wheat glutenin with different numbers of the consensus repeat motifs PGQGQQ + GYYPTSLQQ (21, 45, 110, and 203 residues long) and a recombinant 58,000-Da relative molecular mass (Mr 58,000) repetitive peptide from a single subunit (1Dx5) are studied using Fourier transform IR spectroscopy. The spectra of the dry peptides are very similar; at low water contents (

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry
Related URLs:
Depositing User: Rachel Smith
Date Deposited: 24 Feb 2011 10:07
Last Modified: 21 Apr 2020 20:31
URI: https://ueaeprints.uea.ac.uk/id/eprint/21271
DOI: 10.1002/bip.10298

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