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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Andrade, Fabiana Diuk [1] ; Newson, William R. [2] ; Bernardinelli, Oigres Daniel [1] ; Rasheed, Faiza [2] ; Cobo, Marcio Fernando [1] ; Plivelic, Tomas S. [3] ; deAzevedo, Eduardo Ribeiro [1] ; Kuktaite, Ramune [2]
Total Authors: 8
Affiliation:
[1] Univ Sao Paulo, Inst Fis Sao Carlos, CP 369, BR-13660970 Sao Carlos, SP - Brazil
[2] Swedish Univ Agr Sci, Dept Plant Breeding, POB 101, SE-23053 Alnarp - Sweden
[3] Lund Univ, MAX Lab 4, Fotongatan 2, SE-22592 Lund - Sweden
Total Affiliations: 3
Document type: Journal article
Source: JOURNAL OF POLYMER SCIENCE PART B-POLYMER PHYSICS; v. 56, n. 9, p. 739-750, MAY 1 2018.
Web of Science Citations: 2
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 -sheets and disordered structures, while decreasing -helices in Gli/Glu-glycerol blends studied by C-13 CPMAS NMR. For 20% glycerol samples, the protein side-chain mobility increased similarly for Gli and Glu. A higher proportion of -helices versus -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. (c) 2018 Wiley Periodicals, Inc. J. Polym. Sci., Part B: Polym. Phys. 2018, 56, 739-750 (AU)

FAPESP's process: 11/14099-3 - Use of Time Domain - NMR for the characterization of high viscosity organic systems
Grantee:Fabiana Diuk de Andrade
Support Opportunities: Scholarships in Brazil - Post-Doctoral