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- W2034291803 abstract "The interaction of the lexA repressor of E. coli with poly[d(A-T)] has been studied by circular dichroism. The binding induces an about 2-fold increase of the circular dichroism intensity at 263 nm, pointing out a conformational change of the nucleic acid. The observed spectral changes are very similar to those observed for the binding of the lac repressor to poly[d(A-T)] and natural DNA. At elevated ionic strength the binding isotherms do show a pronounced sigmoidal shape indicating a cooperative mode of binding." @default.
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- W2034291803 date "1984-06-11" @default.
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- W2034291803 title "Cooperative and salt-resistant binding of LexA protein to non-operator DNA" @default.
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- W2034291803 doi "https://doi.org/10.1016/0014-5793(84)80489-5" @default.
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