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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

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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Autor(es):
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]
Número total de Autores: 8
Afiliação do(s) autor(es):
[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
Número total de Afiliações: 3
Tipo de documento: Artigo Científico
Fonte: JOURNAL OF POLYMER SCIENCE PART B-POLYMER PHYSICS; v. 56, n. 9, p. 739-750, MAY 1 2018.
Citações Web of Science: 2
Resumo

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)

Processo FAPESP: 11/14099-3 - Uso de RMN no domínio do tempo para caracterização de sistemas orgânicos de alta viscosidade
Beneficiário:Fabiana Diuk de Andrade
Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado