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

K. A. Feeney; N. Wellner; S. M. Gilbert; N. G. Halford; A. S. Tatham; P. R. Shewry; Peter Belton

doi:10.1002/bip.10298

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

K. A. Feeney, N. Wellner, S. M. Gilbert, N. G. Halford, A. S. Tatham, P. R. Shewry, Peter Belton

School of Chemistry

Research output: Contribution to journal › Article › peer-review

81 Citations (Scopus)

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 (

Original language	English
Pages (from-to)	123-131
Number of pages	9
Journal	Biopolymers
Volume	72
Issue number	2
DOIs	https://doi.org/10.1002/bip.10298
Publication status	Published - 2003

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10.1002/bip.10298

Cite this

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title = "Molecular structures and interactions of repetitive peptides based on wheat glutenin subunits depend on chain length",

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 (",

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AU - Feeney, K. A.

AU - Wellner, N.

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AU - Tatham, A. S.

AU - Shewry, P. R.

AU - Belton, Peter

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AB - 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 (

U2 - 10.1002/bip.10298

DO - 10.1002/bip.10298

M3 - Article

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EP - 131

JO - Biopolymers

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