An insight into molecular motions and phase composition of gliadin/glutenin glycerol blends studied by 13C solid-state and 1H time-domain NMR
(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.
(Less)
- author
- Diuk Andrade, Fabiana ; Newson, William R. ; Bernardinelli, Oigres Daniel ; Rasheed, Faiza ; Cobo, Márcio Fernando ; Plivelic, Tomás S. LU ; Ribeiro deAzevedo, Eduardo and Kuktaite, Ramune
- organization
- publishing date
- 2018-05-01
- 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 Inc.
- 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
- 2022-04-09 23:33:46
@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}}, keywords = {{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 Inc.}}, 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}}, doi = {{10.1002/polb.24586}}, volume = {{56}}, year = {{2018}}, }