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Structural architec...
Structural architecture and solubility of native and modified gliadin and glutenin proteins : non-crystalline molecular and atomic organization
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- Rasheed, Faiza (författare)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för växtförädling,Department of Plant Breeding
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- Newson, William (författare)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för växtförädling,Department of Plant Breeding
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Plivelic, Tomas S. (författare)
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- Kuktaite, Ramune (författare)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för växtförädling,Department of Plant Breeding
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- Hedenqvist, Mikael S. (författare)
- KTH,Polymera material
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- Gällstedt, Mikael (författare)
- RISE,Innventia
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- Johansson, Eva (författare)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för växtförädling,Department of Plant Breeding
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(creator_code:org_t)
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- 2014
- 2014
- Engelska.
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Ingår i: RSC Advances. - 2046-2069. ; 4:4, s. 2051-2060
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://res.slu.se/i...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- 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 packed (HCP) assemblies with lattice parameter of (58 angstrom) 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 beta-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 plastic materials, foams, adhesives, films and coatings.
Ämnesord
- NATURVETENSKAP -- Kemi -- Annan kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Other Chemistry Topics (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
- NATURVETENSKAP -- Fysik -- Atom- och molekylfysik och optik (hsv//swe)
- NATURAL SCIENCES -- Physical Sciences -- Atom and Molecular Physics and Optics (hsv//eng)
Nyckelord
- Experimental evidence
- Hexagonal closed packed (hcp)
- Molecular arrangements
- Organized structure
- Proteins structures
- Structural architecture
- Structural modifications
- Tertiary structures
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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