Probing the folding pathway of a consensus serpin using single tryptophan mutants

HIGHLIGHTS

  • who: Li Yang from the (UNIVERSITY) have published the research: Probing the folding pathway of a consensus serpin using single tryptophan mutants, in the Journal: (JOURNAL) of 14/06/2017

SUMMARY

    The authors have designed a version of conserpin, cAT, with the inhibitory specificity of α1-antitrypsin, and generated single-tryptophan variants to probe its folding pathway in more detail. cAT exhibited similar thermal stability to the parental protein, an inactivation associated with oligomerisation rather a transition to the latent conformation, and a native state with pronounced kinetic stability. A combination of intrinsic . . .

     

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