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 | Acesso ao texto completo restrito à biblioteca da Embrapa Pecuária Sudeste. Para informações adicionais entre em contato com cppse.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Pecuária Sudeste. |
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Data corrente: |
23/01/2006 |
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Data da última atualização: |
08/05/2023 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
BICUDO, T. C.; FORATO, L. A.; BATISTA, L. A. R.; COLNAGO, L. A. |
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Afiliação: |
TATIANA C. BICUDO; LUCIMARA A. FORATO; LUIZ ALBERTO ROCHA BATISTA, CPPSE; LUIZ ALBERTO COLNAGO, CNPDIA. |
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Título: |
Study of the conformation of Y-zeins in purifield maize protein bodies by FTIR and NMR spectroscopy. |
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Ano de publicação: |
2005 |
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Fonte/Imprenta: |
Analytical and Bioanlytical Chemistry, v. 383, p. 291-296, 2005. |
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DOI: |
10.1007/s00216-005-0003-z |
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Idioma: |
Inglês |
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Conteúdo: |
The gamma-zeins are a mixture of 16, 27, and 50-kDa polypeptides which are important in the formation and stabilization of protein bodies (PB). These organelles are used for deposition of zeins, the water-insoluble storage proteins in maize. The nature of the physical interaction between proteins in the assembly and stabilization of PB are fairly well known. It is suggested the repeated hexapeptide sequence (PPPVHL)(8) in the N-terminus is responsible for aggregation of the gamma-zeins on the PB surface. Despite this importance, there is little information about the native conformation of gamma-zeins. In this work, we have analyzed the secondary structures of gamma-zeins in purified protein bodies from two maize cultivars, in the solid state, by FTIR and NMR spectroscopy. The results revealed that gamma-zeins in their physiological state are comprise similar proportions of alpha-helix and beta-sheet, 33 and 31% as determined by FTIR. It was not possible to state if the polyproline II (PPII) conformation is present in the solid-state structure of gamma-zeins, as has been demonstrated for the hexapeptide in solution. Because of the similarity of the solid-state NMR spectra of gamma and alpha-zeins in the alpha carbon region we attributed their contributions to the beta-sheet structures rather than to the PPII conformation or a mixture of these extended structures. |
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Palavras-Chave: |
FTIR; Solid state NMR; Y Zeins. |
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Thesaurus Nal: |
Protein bodies; Protein secondary structure. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 02089naa a2200229 a 4500
001 1047274
005 2023-05-08
008 2005 bl uuuu u00u1 u #d
024 7 $a10.1007/s00216-005-0003-z$2DOI
100 1 $aBICUDO, T. C.
245 $aStudy of the conformation of Y-zeins in purifield maize protein bodies by FTIR and NMR spectroscopy.$h[electronic resource]
260 $c2005
520 $aThe gamma-zeins are a mixture of 16, 27, and 50-kDa polypeptides which are important in the formation and stabilization of protein bodies (PB). These organelles are used for deposition of zeins, the water-insoluble storage proteins in maize. The nature of the physical interaction between proteins in the assembly and stabilization of PB are fairly well known. It is suggested the repeated hexapeptide sequence (PPPVHL)(8) in the N-terminus is responsible for aggregation of the gamma-zeins on the PB surface. Despite this importance, there is little information about the native conformation of gamma-zeins. In this work, we have analyzed the secondary structures of gamma-zeins in purified protein bodies from two maize cultivars, in the solid state, by FTIR and NMR spectroscopy. The results revealed that gamma-zeins in their physiological state are comprise similar proportions of alpha-helix and beta-sheet, 33 and 31% as determined by FTIR. It was not possible to state if the polyproline II (PPII) conformation is present in the solid-state structure of gamma-zeins, as has been demonstrated for the hexapeptide in solution. Because of the similarity of the solid-state NMR spectra of gamma and alpha-zeins in the alpha carbon region we attributed their contributions to the beta-sheet structures rather than to the PPII conformation or a mixture of these extended structures.
650 $aProtein bodies
650 $aProtein secondary structure
653 $aFTIR
653 $aSolid state NMR
653 $aY Zeins
700 1 $aFORATO, L. A.
700 1 $aBATISTA, L. A. R.
700 1 $aCOLNAGO, L. A.
773 $tAnalytical and Bioanlytical Chemistry$gv. 383, p. 291-296, 2005.
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Registro original: |
Embrapa Pecuária Sudeste (CPPSE) |
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| Registros recuperados : 10 | |
| 7. |  | BICUDO, R. C.; BICUDO, T. C.; FORATO, L. A.; TITATO, G. M.; COLNAGO, L. A.; LANÇAS, F. M. Identification of non-zein proteins in BR473 maize protein bodies by LC-nanoESI-MS/MS. Journal of separation science, Weinheim, v. 32, p. 3579-3584, 2009.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Instrumentação. |
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| 8. | | BICUDO, T. C.; BICUDO, R. C.; FORATO, L. A.; BELTRAMINI, L. M.; BATISTA, L. A. R.; BERNARDES FILHO, R.; COLNAGO, L. A. Gamma-zein secondary structure in solution by circular dichroism. Biopolymers, New York, v. 89, n. 3, p. 175-178, 2008.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: Internacional - A |
| Biblioteca(s): Embrapa Instrumentação. |
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| 9. | | BICUDO, T. C.; BICUDO, R. C.; FORATO, L. A.; BELTRAMINI, L. M.; BATISTA, L. A. R.; BERNARDES FILHO, R.; COLNAGO, L. A. y-Zein secondary structure in solution by circular dichroism. Biopolymers, v. 89, n. 3, p. 175-178, mar. 2008.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: Internacional - A |
| Biblioteca(s): Embrapa Pecuária Sudeste. |
|  |
| 10. | | BICUDO, T. C.; BICUDO, R. C.; FORATO, L. A.; BELTRAMINI, L. M.; BATISTA, L. A. R.; BERNARDES FILHO, R.; COLNAGO, L. A. Zein secondary structure in solution by circular dichroism. Biopolymers, New York, v. 89, n. 3, p. 175-178, 2007.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: Internacional - A |
| Biblioteca(s): Embrapa Instrumentação. |
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| Registros recuperados : 10 | |
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| Nenhum registro encontrado para a expressão de busca informada. |
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