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- W2078281211 abstract "Abstract In an attempt to elucidate the mechanism of assembly of the bacteriophage fd we examined the interaction between the coat protein (B-protein) and the gene-5-protein-DNA-complex, using the heterologous crosslinking reagent methyl-4-azidobenzoimidate (MABI). An interaction between the two proteins would yield a crosslinked associate. This reaction has been performed at different conditions, the results of which were not conclusive and are discussed. We furthermore report an investigation of the association properties of the B-protein itself. We used the energy transfer between B-protein species differently labeled with a yellow dye ( N -iodoacetyl- N ′-(8-sulfo-1-naphthyl)ethylenediamine) or with a red dye (trichloropyrimidinyl reactive red) to monitor the mode of association of the protein in different solvents. The dimer of the B-protein seems to be the building unit of the string-like aggregates, whereas with guanidinium chloride and dodecylsulfate a dissociation of the dimers and recombination (on dilution) into individual oligomers is possible." @default.
- W2078281211 created "2016-06-24" @default.
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- W2078281211 date "1980-01-01" @default.
- W2078281211 modified "2023-09-24" @default.
- W2078281211 title "Tentative approach to investigate the mechanism of the bacteriophage fd assembly" @default.
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- W2078281211 doi "https://doi.org/10.1016/0303-2647(80)90017-9" @default.
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