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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: |
02/03/2010 |
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Autoria: |
COLNAGO, L. A.; LEO, G. C.; VALENTINE, K. G.; OPELLA, S. J. |
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Afiliação: |
EMBRAPA-CNPDIA; University of Pennsylvania. |
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Título: |
Direct comparison of the membrane bound and structural forms of the coat protein of the filamentous bacteriophage fd. |
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Ano de publicação: |
1986 |
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Fonte/Imprenta: |
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. |
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Páginas: |
p. 147 - 158 |
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Idioma: |
Inglês |
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Conteúdo: |
The coat protein of the filamentous bacteriophage fd exists in a membrane bound form as well as in the structural form of the virus during its lifecycle. The changes in the dynamics of the coat protein that accompany the infection of E. coli and the assembly new virus particles are described with NMR experiments. Solid state NMR is used to describe the dynamics of isotopically labelled peptide backbone and amino acid sidechain sites. Motional averaging of powder pattern lineshapes gives qualitative information about the amplitudes and rates of motions. |
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Palavras-Chave: |
Coat protein; Fd; Filamentous bacteriophage; Membrane bound. |
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Categoria do assunto: |
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Marc: |
LEADER 01383naa a2200217 a 4500
001 1026590
005 2010-03-02
008 1986 bl --- 0-- u #d
100 1 $aCOLNAGO, L. A.
245 $aDirect comparison of the membrane bound and structural forms of the coat protein of the filamentous bacteriophage fd.
260 $c1986
300 $ap. 147 - 158
520 $aThe coat protein of the filamentous bacteriophage fd exists in a membrane bound form as well as in the structural form of the virus during its lifecycle. The changes in the dynamics of the coat protein that accompany the infection of E. coli and the assembly new virus particles are described with NMR experiments. Solid state NMR is used to describe the dynamics of isotopically labelled peptide backbone and amino acid sidechain sites. Motional averaging of powder pattern lineshapes gives qualitative information about the amplitudes and rates of motions.
653 $aCoat protein
653 $aFd
653 $aFilamentous bacteriophage
653 $aMembrane bound
700 1 $aLEO, G. C.
700 1 $aVALENTINE, K. G.
700 1 $aOPELLA, S. J.
773 $tIn: 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.
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Registro original: |
Embrapa Instrumentação (CNPDIA) |
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| Registros recuperados : 3 | |
| 1. |  | 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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| Registros recuperados : 3 | |
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