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Registro Completo |
Biblioteca(s): |
Embrapa Pecuária Sudeste. |
Data corrente: |
23/01/2006 |
Data da última atualização: |
08/05/2023 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
BICUDO, T. C.; FORATO, L. A.; BATISTA, L. A. R.; COLNAGO, L. A. |
Afiliação: |
TATIANA C. BICUDO; LUCIMARA A. FORATO; LUIZ ALBERTO ROCHA BATISTA, CPPSE; LUIZ ALBERTO COLNAGO, CNPDIA. |
Título: |
Study of the conformation of Y-zeins in purifield maize protein bodies by FTIR and NMR spectroscopy. |
Ano de publicação: |
2005 |
Fonte/Imprenta: |
Analytical and Bioanlytical Chemistry, v. 383, p. 291-296, 2005. |
DOI: |
10.1007/s00216-005-0003-z |
Idioma: |
Inglês |
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. |
Palavras-Chave: |
FTIR; Solid state NMR; Y Zeins. |
Thesaurus Nal: |
Protein bodies; Protein secondary structure. |
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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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Embrapa Pecuária Sudeste (CPPSE) |
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Registro Completo
Biblioteca(s): |
Embrapa Agrobiologia. |
Data corrente: |
25/02/2013 |
Data da última atualização: |
14/05/2014 |
Tipo da produção científica: |
Comunicado Técnico/Recomendações Técnicas |
Autoria: |
OLIVEIRA, E. A. G. de; RIBEIRO, R. de L. D.; GUERRA, J. G. M.; LEAL, M. A. de A.; ESPINDOLA, J. A. A.; ARAUJO, E. da S. |
Afiliação: |
EVA ADRIANA DE OLIVEIRA, UFRRJ; Raul de Lucena Duarte Ribeiro; JOSE GUILHERME MARINHO GUERRA, CNPAB; MARCO ANTONIO DE ALMEIDA LEAL, CNPAB; JOSE ANTONIO AZEVEDO ESPINDOLA, CNPAB; EDNALDO DA SILVA ARAUJO, CNPAB. |
Título: |
Substrato produzido a partir de fontes renováveis para a produção orgânica de mudas de hortaliças. |
Ano de publicação: |
2011 |
Fonte/Imprenta: |
Seropédica: Embrapa Agrobiologia, 2011. |
Páginas: |
4p. |
Série: |
(Embrapa agrobiologia. Comunicado Ténico, 134) |
Idioma: |
Português |
Thesagro: |
Adubo Orgânico. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/92126/1/COT134-11.pdf
|
Marc: |
LEADER 00625nam a2200193 a 4500 001 1950875 005 2014-05-14 008 2011 bl uuuu u0uu1 u #d 100 1 $aOLIVEIRA, E. A. G. de 245 $aSubstrato produzido a partir de fontes renováveis para a produção orgânica de mudas de hortaliças. 260 $aSeropédica: Embrapa Agrobiologia$c2011 300 $a4p. 490 $a(Embrapa agrobiologia. Comunicado Ténico, 134) 650 $aAdubo Orgânico 700 1 $aRIBEIRO, R. de L. D. 700 1 $aGUERRA, J. G. M. 700 1 $aLEAL, M. A. de A. 700 1 $aESPINDOLA, J. A. A. 700 1 $aARAUJO, E. da S.
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