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An insight into molecular motions and phase composition of gliadin/glutenin glycerol blends studied by 13C solid-state and 1H time-domain NMR

Diuk Andrade, Fabiana; Newson, William R.; Bernardinelli, Oigres Daniel; Rasheed, Faiza; Cobo, Márcio Fernando; Plivelic, Tomás S. LU ; Ribeiro deAzevedo, Eduardo and Kuktaite, Ramune (2018) In Journal of Polymer Science, Part B: Polymer Physics 56(9). p.739-750
Abstract

Monitoring of the molecular motions and secondary structures of gliadin (Gli) and glutenin (Glu) in blends with 10, 20, 30, and 40% glycerol was performed by solid-state (SS) and time domain (TD) NMR spectroscopy. Increasing the glycerol content increased the relative amount of β-sheets and disordered structures, while decreasing α-helices in Gli/Glu–glycerol blends studied by 13C CPMAS NMR. For ≥20% glycerol samples, the protein side-chain mobility increased similarly for Gli and Glu. A higher proportion of α-helices versus β-sheets was found in Gli-glycerol blends compared with Glu–glycerol blends. Glycerol acted as “immobilized” in 10–20% glycerol Gli samples and was found mainly “free” in 30 and 40% glycerol Gli/Glu... (More)

Monitoring of the molecular motions and secondary structures of gliadin (Gli) and glutenin (Glu) in blends with 10, 20, 30, and 40% glycerol was performed by solid-state (SS) and time domain (TD) NMR spectroscopy. Increasing the glycerol content increased the relative amount of β-sheets and disordered structures, while decreasing α-helices in Gli/Glu–glycerol blends studied by 13C CPMAS NMR. For ≥20% glycerol samples, the protein side-chain mobility increased similarly for Gli and Glu. A higher proportion of α-helices versus β-sheets was found in Gli-glycerol blends compared with Glu–glycerol blends. Glycerol acted as “immobilized” in 10–20% glycerol Gli samples and was found mainly “free” in 30 and 40% glycerol Gli/Glu samples. During temperature experiments, 30 and 40% glycerol amounts impacted the dynamic molecular behavior of the Gli and Glu proteins differently than lipids, as observed by TD-NMR. The combination of TD-NMR together with SS-NMR showed details of the dynamic molecular variations in Gli/Glu protein structure and are promising techniques to monitor the molecular dynamics of plasticized proteins.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
biopolymers, films, gliadin, glutenin, molecular dynamics, NMR, protein secondary structure, renewable resources, structural dynamics, structure-property relations
in
Journal of Polymer Science, Part B: Polymer Physics
volume
56
issue
9
pages
12 pages
publisher
John Wiley & Sons
external identifiers
  • scopus:85043360977
ISSN
0887-6266
DOI
10.1002/polb.24586
language
English
LU publication?
yes
id
527a0de4-3fd4-4f94-8462-81fa70b04fe5
date added to LUP
2018-05-03 07:53:10
date last changed
2018-05-29 09:18:17
@article{527a0de4-3fd4-4f94-8462-81fa70b04fe5,
  abstract     = {<p>Monitoring of the molecular motions and secondary structures of gliadin (Gli) and glutenin (Glu) in blends with 10, 20, 30, and 40% glycerol was performed by solid-state (SS) and time domain (TD) NMR spectroscopy. Increasing the glycerol content increased the relative amount of β-sheets and disordered structures, while decreasing α-helices in Gli/Glu–glycerol blends studied by <sup>13</sup>C CPMAS NMR. For ≥20% glycerol samples, the protein side-chain mobility increased similarly for Gli and Glu. A higher proportion of α-helices versus β-sheets was found in Gli-glycerol blends compared with Glu–glycerol blends. Glycerol acted as “immobilized” in 10–20% glycerol Gli samples and was found mainly “free” in 30 and 40% glycerol Gli/Glu samples. During temperature experiments, 30 and 40% glycerol amounts impacted the dynamic molecular behavior of the Gli and Glu proteins differently than lipids, as observed by TD-NMR. The combination of TD-NMR together with SS-NMR showed details of the dynamic molecular variations in Gli/Glu protein structure and are promising techniques to monitor the molecular dynamics of plasticized proteins.</p>},
  author       = {Diuk Andrade, Fabiana and Newson, William R. and Bernardinelli, Oigres Daniel and Rasheed, Faiza and Cobo, Márcio Fernando and Plivelic, Tomás S. and Ribeiro deAzevedo, Eduardo and Kuktaite, Ramune},
  issn         = {0887-6266},
  keyword      = {biopolymers,films,gliadin,glutenin,molecular dynamics,NMR,protein secondary structure,renewable resources,structural dynamics,structure-property relations},
  language     = {eng},
  month        = {05},
  number       = {9},
  pages        = {739--750},
  publisher    = {John Wiley & Sons},
  series       = {Journal of Polymer Science, Part B: Polymer Physics},
  title        = {An insight into molecular motions and phase composition of gliadin/glutenin glycerol blends studied by <sup>13</sup>C solid-state and <sup>1</sup>H time-domain NMR},
  url          = {http://dx.doi.org/10.1002/polb.24586},
  volume       = {56},
  year         = {2018},
}