Molecular structures and interactions of repetitive peptides based on HMW subunit 1Dx5

Peter R. Shewry; Arthur S. Tatham; N. Wellner; S. Gilbert; K. Feeney; Peter S. Belton

doi:10.1039/9781847552372

Molecular structures and interactions of repetitive peptides based on HMW subunit 1Dx5

Peter R. Shewry, Arthur S. Tatham, N. Wellner, S. Gilbert, K. Feeney, Peter S. Belton

School of Chemistry

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

A characteristic feature of high molecular weight (HMW) subunits, as with many gluten proteins, is their large repetitive central domain. This consists of tandem and interspersed repeats based on two or three consensus motifs: a nonapeptide (Gly . T yr .T yr .Pro .Thr . S er .Pro/Leu. Gln. Gln), a hexapeptide (Pro .Gly . Gln. Gly . Gln. Gln) and, in the x-type subunits only, a tripeptide (Gly.Gln.Gln). Secondary structure prediction and spectroscopic studies of purified HMW subunits and short synthetic peptides based on the consensus repeat motifs have indicated that in solution the repetitive domain forms a loose spiral consisting of regularly repeated preverse turns’”. In the solid state numerous non-covalent intermolecular interactions exist. We have used Fourier-transform infrared spectroscopy to study perfect repeat peptides with different lengths in order to understand how this affects the molecular structures.

Original language	English
Title of host publication	Wheat Gluten
Publisher	Royal Society of Chemistry
Pages	183-187
Number of pages	5
ISBN (Print)	978-1-84755-237-2
DOIs	https://doi.org/10.1039/9781847552372 https://doi.org/10.1039/9781847552372-00183
Publication status	Published - 2000

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title = "Molecular structures and interactions of repetitive peptides based on HMW subunit 1Dx5",

abstract = "A characteristic feature of high molecular weight (HMW) subunits, as with many gluten proteins, is their large repetitive central domain. This consists of tandem and interspersed repeats based on two or three consensus motifs: a nonapeptide (Gly . T yr .T yr .Pro .Thr . S er .Pro/Leu. Gln. Gln), a hexapeptide (Pro .Gly . Gln. Gly . Gln. Gln) and, in the x-type subunits only, a tripeptide (Gly.Gln.Gln). Secondary structure prediction and spectroscopic studies of purified HMW subunits and short synthetic peptides based on the consensus repeat motifs have indicated that in solution the repetitive domain forms a loose spiral consisting of regularly repeated preverse turns{\textquoteright}”. In the solid state numerous non-covalent intermolecular interactions exist. We have used Fourier-transform infrared spectroscopy to study perfect repeat peptides with different lengths in order to understand how this affects the molecular structures.",

author = "Shewry, {Peter R.} and Tatham, {Arthur S.} and N. Wellner and S. Gilbert and K. Feeney and Belton, {Peter S.}",

year = "2000",

doi = "10.1039/9781847552372",

language = "English",

isbn = "978-1-84755-237-2",

pages = "183--187",

booktitle = "Wheat Gluten",

publisher = "Royal Society of Chemistry",

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TY - CHAP

T1 - Molecular structures and interactions of repetitive peptides based on HMW subunit 1Dx5

AU - Shewry, Peter R.

AU - Tatham, Arthur S.

AU - Wellner, N.

AU - Gilbert, S.

AU - Feeney, K.

AU - Belton, Peter S.

PY - 2000

Y1 - 2000

N2 - A characteristic feature of high molecular weight (HMW) subunits, as with many gluten proteins, is their large repetitive central domain. This consists of tandem and interspersed repeats based on two or three consensus motifs: a nonapeptide (Gly . T yr .T yr .Pro .Thr . S er .Pro/Leu. Gln. Gln), a hexapeptide (Pro .Gly . Gln. Gly . Gln. Gln) and, in the x-type subunits only, a tripeptide (Gly.Gln.Gln). Secondary structure prediction and spectroscopic studies of purified HMW subunits and short synthetic peptides based on the consensus repeat motifs have indicated that in solution the repetitive domain forms a loose spiral consisting of regularly repeated preverse turns’”. In the solid state numerous non-covalent intermolecular interactions exist. We have used Fourier-transform infrared spectroscopy to study perfect repeat peptides with different lengths in order to understand how this affects the molecular structures.

AB - A characteristic feature of high molecular weight (HMW) subunits, as with many gluten proteins, is their large repetitive central domain. This consists of tandem and interspersed repeats based on two or three consensus motifs: a nonapeptide (Gly . T yr .T yr .Pro .Thr . S er .Pro/Leu. Gln. Gln), a hexapeptide (Pro .Gly . Gln. Gly . Gln. Gln) and, in the x-type subunits only, a tripeptide (Gly.Gln.Gln). Secondary structure prediction and spectroscopic studies of purified HMW subunits and short synthetic peptides based on the consensus repeat motifs have indicated that in solution the repetitive domain forms a loose spiral consisting of regularly repeated preverse turns’”. In the solid state numerous non-covalent intermolecular interactions exist. We have used Fourier-transform infrared spectroscopy to study perfect repeat peptides with different lengths in order to understand how this affects the molecular structures.

U2 - 10.1039/9781847552372

DO - 10.1039/9781847552372

M3 - Chapter

SN - 978-1-84755-237-2

SP - 183

EP - 187

BT - Wheat Gluten

PB - Royal Society of Chemistry

ER -