A partially folded intermediate conformation is induced in pectate lyase C by the addition of 8-anilino-1-naphthalenesulfonate (ANS).

作者: Douglas E. Kamen , Robert W. Woody

DOI: 10.1110/PS.19801

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摘要: Addition of 8-anilino-1-naphthalenesulfonate (ANS) to acid-denatured pectate lyase C (pelC) leads a large increase in the fluorescence quantum yield near 480 nm. The conventional interpretation such an observation is that ANS binding partially folded intermediate as molten globule. Far-ultraviolet circular dichroism demonstrates enhanced results from induction protein species adopts fraction native-like secondary structure on ANS. Thus, does not act probe detect species, but induces species. Near-ultraviolet suggests bound specific conformation. mechanism and was probed. interaction acid-unfolded pelC with several analogs investigated. strongly indicate combined effects hydrophobic electrostatic interactions account for relatively high affinity pelC. These demonstrate need caution interpreting enhancement evidence presence globule or other intermediates.

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