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- W1978266114 abstract "The interaction between DNA and the structural protein IV of bacteriophage PM2 was studied by co-sedimentation, filter binding and electron microscopy. The co-sedimentation data and the sigmoid-shaped filter binding curve were interpreted in terms of co-operative binding. At a given DNA/protein input ratio, some DNA molecules were associated with a large amount of protein IV while others had no detectable protein bound to them. Electron microscopic examination of DNA-protein IV mixtures showed highly condensed DNA molecules alongside uncomplexed native DNA. Dissociation experiments revealed the presence of two types of complexes. Type I dissociated rapidly while type II had a long half-life. Dissociation of complexes obtained with increasing protein/DNA ratios suggested that the type I complex was a precursor of type II complex. Protein IV binds equally well to superhelical, relaxed or linear DNA as well as to single-stranded DNA. These observations lead to a model for the interaction and for the consequent alterations in the DNA structure." @default.
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- W1978266114 date "1979-06-01" @default.
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- W1978266114 title "Interaction between bacteriophage PM2 protein IV and DNA" @default.
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- W1978266114 doi "https://doi.org/10.1016/0022-2836(79)90303-6" @default.
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