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Registro Completo |
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Biblioteca(s): |
Embrapa Gado de Leite. |
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Data corrente: |
30/04/2015 |
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Data da última atualização: |
22/03/2024 |
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Tipo da produção científica: |
Artigo em Anais de Congresso |
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Autoria: |
CARVALHO, C. O.; SANTOS, A. C. dos; CARVALHO, G. R. |
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Afiliação: |
C. O. CARVALHO; A. C. DOS SANTOS, UFLA; GLAUCO RODRIGUES CARVALHO, CNPGL. |
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Título: |
Rede Brasil Rural: uma nova forma de comercialização para a agricultura familiar. |
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Ano de publicação: |
2012 |
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Fonte/Imprenta: |
In: CONGRESSO DA SOCIEDADE BRASILEIRA DE ECONOMIA, ADMINISTRAÇÃO E SOCIOLOGIA RURAL, 50., 2012, Vitória. Agricultura e desenvolvimento rural com sustentabilidade. Vitória: Sociedade Brasileira de Economia, Administração e Sociologia Rural, 2012. |
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Descrição Física: |
1 CD-ROM. |
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Idioma: |
Português |
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Palavras-Chave: |
Comercialização agrícola; Comercialização eletronica; Rede Brasil Rural. |
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Thesagro: |
Agricultura Familiar. |
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Categoria do assunto: |
E Economia e Indústria Agrícola |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1014768/1/Rede-Brasil-Rural.pdf
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Marc: |
LEADER 00796nam a2200181 a 4500
001 2014768
005 2024-03-22
008 2012 bl uuuu u00u1 u #d
100 1 $aCARVALHO, C. O.
245 $aRede Brasil Rural$buma nova forma de comercialização para a agricultura familiar.$h[electronic resource]
260 $aIn: CONGRESSO DA SOCIEDADE BRASILEIRA DE ECONOMIA, ADMINISTRAÇÃO E SOCIOLOGIA RURAL, 50., 2012, Vitória. Agricultura e desenvolvimento rural com sustentabilidade. Vitória: Sociedade Brasileira de Economia, Administração e Sociologia Rural$c2012
300 $c1 CD-ROM.
650 $aAgricultura Familiar
653 $aComercialização agrícola
653 $aComercialização eletronica
653 $aRede Brasil Rural
700 1 $aSANTOS, A. C. dos
700 1 $aCARVALHO, G. R.
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Registro original: |
Embrapa Gado de Leite (CNPGL) |
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Registro Completo
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
15/02/2005 |
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Data da última atualização: |
29/05/2018 |
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Autoria: |
TIROLI, A. O.; TASIC, L.; OLIVEIRA, C. L. P.; BLOCH JUNIOR, C.; TORRIANI, I.; FARAH, C. S.; RAMOS, C. H. I. |
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Título: |
Mapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of a single-chain chimeras. |
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Ano de publicação: |
2005 |
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Fonte/Imprenta: |
The FEBS Journal, v. 272, n. 2, p. 779-790, 2005. |
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Idioma: |
Inglês |
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Conteúdo: |
The troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnITnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 191 of TnC linked to residues 98182 or 98147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. On the other hand the TnI inhibitory and C-terminal domains were completely digested by trypsin in the absence of calcium while the addition of calcium results in the protection of only residues 114137. MenosThe troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnITnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 191 of TnC linked to residues 98182 or 98147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. O... Mostrar Tudo |
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Palavras-Chave: |
Muscle. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/177877/1/ID-24788.pdf
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Marc: |
LEADER 02317naa a2200205 a 4500
001 1185506
005 2018-05-29
008 2005 bl uuuu u00u1 u #d
100 1 $aTIROLI, A. O.
245 $aMapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of a single-chain chimeras.$h[electronic resource]
260 $c2005
520 $aThe troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnITnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 191 of TnC linked to residues 98182 or 98147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. On the other hand the TnI inhibitory and C-terminal domains were completely digested by trypsin in the absence of calcium while the addition of calcium results in the protection of only residues 114137.
653 $aMuscle
700 1 $aTASIC, L.
700 1 $aOLIVEIRA, C. L. P.
700 1 $aBLOCH JUNIOR, C.
700 1 $aTORRIANI, I.
700 1 $aFARAH, C. S.
700 1 $aRAMOS, C. H. I.
773 $tThe FEBS Journal$gv. 272, n. 2, p. 779-790, 2005.
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Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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