Use este identificador para citar ou linkar para este item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/26590
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dc.contributor.authorCOLNAGO, L. A.
dc.contributor.authorLEO, G. C.
dc.contributor.authorVALENTINE, K. G.
dc.contributor.authorOPELLA, S. J.
dc.date.accessioned2025-04-09T14:48:06Z-
dc.date.available2025-04-09T14:48:06Z-
dc.date.created1999-12-22
dc.date.issued1986
dc.identifier.citationIn: 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.
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/26590-
dc.descriptionThe 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.
dc.language.isoeng
dc.rightsopenAccess
dc.subjectCoat protein
dc.subjectMembrane bound
dc.subjectFilamentous bacteriophage
dc.subjectFd
dc.titleDirect comparison of the membrane bound and structural forms of the coat protein of the filamentous bacteriophage fd.
dc.typeResumo em anais e proceedings
dc.format.extent2p. 147 - 158
riaa.ainfo.id26590
riaa.ainfo.lastupdate2025-04-09
dc.contributor.institutionEMBRAPA-CNPDIA; University of Pennsylvania.
Aparece nas coleções:Artigo em anais de congresso (CNPDIA)

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