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- W2016565764 abstract "Binding of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) to adenylylated $$E_{overline {11} } $$ glutamine synthetase is cooperative and time-dependent, with 3 dye sites per subunit. In fluorescence polarization experiments TNS and pyrene butyrate give normalized Perrin plots that indicate a symmetrical arrangement of dye excited state dipoles, relative to the rotational axis of the oblate ellipsoid of the dodecameric native enzyme." @default.
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- W2016565764 title "Interaction of extrinic fluoresence probes with E. coli glutamine synthetase" @default.
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