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Structural architecture and solubility of native and modified gliadin and glutenin proteins: non-crystalline molecular and atomic organization

Rasheed, Faiza; Newson, William R.; Plivelic, Tomás LU ; Kuktaite, Ramune; Hedenqvist, Mikael S.; Gällstedt, Mikael and Johansson, Eva (2014) In RSC Advances 4(4). p.2051-2060
Abstract
Wheat gluten (WG) and its components, gliadin and glutenin proteins, form the largest polymers in nature, which complicates the structural architecture of these proteins. Wheat gluten, gliadin and glutenin

proteins in unmodified form showed few secondary structural features. Structural modification of these proteins using heat, pressure and the chemical chaperone glycerol resulted in a shift to organized

structure. In modified gliadin, nano-structural molecular arrangements in the form of hexagonal closed pack (HCP) assemblies with lattice parameter of (58 Å) were obvious together with development of intermolecular disulphide bonds. Modification of glutenin resulted in highly polymerized structure with proteins linked not... (More)
Wheat gluten (WG) and its components, gliadin and glutenin proteins, form the largest polymers in nature, which complicates the structural architecture of these proteins. Wheat gluten, gliadin and glutenin

proteins in unmodified form showed few secondary structural features. Structural modification of these proteins using heat, pressure and the chemical chaperone glycerol resulted in a shift to organized

structure. In modified gliadin, nano-structural molecular arrangements in the form of hexagonal closed pack (HCP) assemblies with lattice parameter of (58 Å) were obvious together with development of intermolecular disulphide bonds. Modification of glutenin resulted in highly polymerized structure with proteins linked not only by disulphide bonds, but also with other covalent and irreversible bonds, as well as the highest proportion of b-sheets. From a combination of experimental evidence and protein algorithms, we have proposed tertiary structure models of unmodified and modified gliadin and glutenin proteins. An increased understanding of gliadin and glutenin proteins structure and behavior are of utmost importance to understand the applicability of these proteins for various applications including plastics materials, foams, adhesives, films and coatings. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
RSC Advances
volume
4
issue
4
pages
2051 - 2060
publisher
Royal Society of Chemistry
external identifiers
  • wos:000329033700070
  • scopus:84890034091
ISSN
2046-2069
DOI
10.1039/c3ra45522j
language
English
LU publication?
yes
id
3c67cc29-9f85-4ba8-afc0-ae8b0fb3a59a (old id 4178278)
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http://pubs.rsc.org/en/content/articlelanding/2013/ra/c3ra45522j#!divAbstract
date added to LUP
2013-11-29 11:03:08
date last changed
2017-01-15 03:55:17
@article{3c67cc29-9f85-4ba8-afc0-ae8b0fb3a59a,
  abstract     = {Wheat gluten (WG) and its components, gliadin and glutenin proteins, form the largest polymers in nature, which complicates the structural architecture of these proteins. Wheat gluten, gliadin and glutenin<br/><br>
proteins in unmodified form showed few secondary structural features. Structural modification of these proteins using heat, pressure and the chemical chaperone glycerol resulted in a shift to organized<br/><br>
structure. In modified gliadin, nano-structural molecular arrangements in the form of hexagonal closed pack (HCP) assemblies with lattice parameter of (58 Å) were obvious together with development of intermolecular disulphide bonds. Modification of glutenin resulted in highly polymerized structure with proteins linked not only by disulphide bonds, but also with other covalent and irreversible bonds, as well as the highest proportion of b-sheets. From a combination of experimental evidence and protein algorithms, we have proposed tertiary structure models of unmodified and modified gliadin and glutenin proteins. An increased understanding of gliadin and glutenin proteins structure and behavior are of utmost importance to understand the applicability of these proteins for various applications including plastics materials, foams, adhesives, films and coatings.},
  author       = {Rasheed, Faiza and Newson, William R. and Plivelic, Tomás and Kuktaite, Ramune and Hedenqvist, Mikael S. and Gällstedt, Mikael and Johansson, Eva},
  issn         = {2046-2069},
  language     = {eng},
  number       = {4},
  pages        = {2051--2060},
  publisher    = {Royal Society of Chemistry},
  series       = {RSC Advances},
  title        = {Structural architecture and solubility of native and modified gliadin and glutenin proteins: non-crystalline molecular and atomic organization},
  url          = {http://dx.doi.org/10.1039/c3ra45522j},
  volume       = {4},
  year         = {2014},
}