Data/hora: 20/06/2024 19:56:09

Biblioteca(s): | Embrapa Instrumentação.
Data corrente: | 22/12/1999
Data da última atualização: | 11/03/2010
Autoria: | COLNAGO, L. A.; OPELLA, S. J.
Afiliação: | EMBRAPA-CNPDIA; University of Pennsylvania.
Título: | Dynamics of the structural and membrane bound forms of filamentous bacteriophage coat protein by deuterium NMR.
Ano de publicação: | 1990
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.
Páginas: | p.146.
Série: | (SBBq Annual Meeting, 19).
Idioma: | Inglês
Notas: | Resumo C-40.
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.
Palavras-Chave: | Bacteriophage; Bound; Coat; Filamentous; Membrane; NMR; Protein; Structure.
Thesaurus Nal: | deuterium; dynamics.
Categoria do assunto: | --
Registro original: | Embrapa Instrumentação (CNPDIA)
Exemplares: | CNPDIA - (5218-1) - UPC - SP - -- - PROCI-90.00009 -  - 1990.00009 - DIS