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| 6. |  | COLNAGO, L. A.; LEO, G. C.; VALENTINE, K. G.; OPELLA, S. J. Direct comparison of the membrane bound and structural forms of the coat protein of the filamentous bacteriophage fd. In: SARMA, R.H.; SARMA, M.H., ed. Biomolecular stereodynamics III: proceedings of the Fourth Conversation in the Discipline Biomolecular Stereodynamics, State University of New York, Albany, NY, June 04-09, 1985. New York: Adenine Press, 1986. p. 147 - 158| Biblioteca(s): Embrapa Instrumentação. |
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| 8. | | COLNAGO, L. A.; MARTIN-NETO, L.; BISCEGLI, C. I.; NASCIMENTO, O. R.; BONAGAMBA, T. J.; PANEPUCCI, H.; VIEIRA, E. M.; SEIDL, P. R.; SPOSITO, G.; OPELLA, S. J. Aplicações da ressonância magnética nuclear (RMN) e ressonância paramagnética eletrônica (EPR). In: CRESTANA, S.; CRUVINEL, P. E.; MASCARENHAS, S.; BISCEGLI, C. I.; MARTIN-NETO, L.; COLNAGO, L. A. (Ed.). Instrumentação agropecuária: contribuições no limiar do novo século. Brasília: EMBRAPA-SPI, 1996. Cap. 1. p.15-50.| Biblioteca(s): Embrapa Instrumentação. |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Instrumentação. Para informações adicionais entre em contato com cnpdia.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Instrumentação. |
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Data corrente: |
22/12/1999 |
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Data da última atualização: |
11/03/2010 |
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Autoria: |
COLNAGO, L. A.; OPELLA, S. J. |
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Afiliação: |
EMBRAPA-CNPDIA; University of Pennsylvania. |
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Título: |
Dynamics of the structural and membrane bound forms of filamentous bacteriophage coat protein by deuterium NMR. |
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Ano de publicação: |
1990 |
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Fonte/Imprenta: |
In: PAN AMERICAN ASSOCIATION OF BIOCHEMICAL SOCIETIES CONGRESS, 6., Feb. 1990, Sao Paulo, SP. Abstracts and program... Sao Paulo: Sociedade Brasileira de Bioquimica, 1990. |
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Páginas: |
p.146. |
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Série: |
(SBBq Annual Meeting, 19). |
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Idioma: |
Inglês |
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Notas: |
Resumo C-40. |
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Conteúdo: |
After infection and prior to assembly, the major coat protein of the filamentous bacteriophages resides within the bacterial cell membrane. This protein is the major structural component of the assembled virus particles. The protein undergoes a major transition between these two biologically important forms that affects the dynamics of a substantial number of residues. Samples of the protein in phospholipid bilayers and in the virus particles are immobile on NMR timescales, therefore solid state 2H NMR studies are useful for describing the internal motions of the protein that occur more frequently than about 10E+6 sec1. Specific sites of residues were labelled biosynthetically with 2H; the lineshapes of the resulting static or motionally averaged powder patterns were analyzed in terms of local motions. These results enable comparisons to be made between the membrane bound and structural forms of coat proteins for fd and Pfl bacteriophages. Fd coat protein has four highly mobile N-terminal residues in the structural form, however the number of mobile residues increases to about ten in the membrane bound form. The Pfl structural form is totally rigid and the membrane bound shows about 10 mobile residues like fd. Many of the aliphatic and aromatic residues with immobile backbone sites in both forms of the protein have large amplitude jump motions that are analyzed in detail through temperature dependence and comparisons of calculated and experimental lineshapes. |
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Palavras-Chave: |
Bacteriophage; Bound; Coat; Filamentous; Membrane; NMR; Protein; Structure. |
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Thesaurus NAL: |
deuterium; dynamics. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02363naa a2200289 a 4500
001 1026604
005 2010-03-11
008 1990 bl --- 0-- u #d
100 1 $aCOLNAGO, L. A.
245 $aDynamics of the structural and membrane bound forms of filamentous bacteriophage coat protein by deuterium NMR.
260 $c1990
300 $ap.146.
490 $a(SBBq Annual Meeting, 19).
500 $aResumo C-40.
520 $aAfter infection and prior to assembly, the major coat protein of the filamentous bacteriophages resides within the bacterial cell membrane. This protein is the major structural component of the assembled virus particles. The protein undergoes a major transition between these two biologically important forms that affects the dynamics of a substantial number of residues. Samples of the protein in phospholipid bilayers and in the virus particles are immobile on NMR timescales, therefore solid state 2H NMR studies are useful for describing the internal motions of the protein that occur more frequently than about 10E+6 sec1. Specific sites of residues were labelled biosynthetically with 2H; the lineshapes of the resulting static or motionally averaged powder patterns were analyzed in terms of local motions. These results enable comparisons to be made between the membrane bound and structural forms of coat proteins for fd and Pfl bacteriophages. Fd coat protein has four highly mobile N-terminal residues in the structural form, however the number of mobile residues increases to about ten in the membrane bound form. The Pfl structural form is totally rigid and the membrane bound shows about 10 mobile residues like fd. Many of the aliphatic and aromatic residues with immobile backbone sites in both forms of the protein have large amplitude jump motions that are analyzed in detail through temperature dependence and comparisons of calculated and experimental lineshapes.
650 $adeuterium
650 $adynamics
653 $aBacteriophage
653 $aBound
653 $aCoat
653 $aFilamentous
653 $aMembrane
653 $aNMR
653 $aProtein
653 $aStructure
700 1 $aOPELLA, S. J.
773 $tIn: PAN AMERICAN ASSOCIATION OF BIOCHEMICAL SOCIETIES CONGRESS, 6., Feb. 1990, Sao Paulo, SP. Abstracts and program... Sao Paulo: Sociedade Brasileira de Bioquimica, 1990.
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