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We hypothesize that (i) the slow inhibition observed in the biochemical assay with the recombinant protein with some of the compounds is due to their preferential binding to a slowly populated conformer of the NADP + -TGR(H) complex and (ii) this conformer is already populated in the worm cell interior accounting for the more rapid inhibition of TGR observed in ex vivo worms with the slow inhibitors

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i.e., highly dynamic sets of many rapidly interconverting, structurally distinct conformations, and this structural fuzziness (inherent structural heterogeneity), is often not a limitation but a fundamental aspect of their functions