Article
Association and activation of fructose 1,6-bisphosphase during unfolding and refolding: spectroscopic and enzymatic studies.
Journal of protein chemistry - 1 Jan 2001
Yuan C, Xie Z Q, Zhang F W, Xu G J
Abstract excerpt
Fructose 1,6-biphosphase is a well-characterized oligomer enzyme, and many effectors allosterically control its activity. In this report, we compared the activity, allosteric properties, and conformational changes in its denaturant-induced unfolding processes. In addition, a trpytophan residue has been introduced into the interface between the C1 and C2 subunits to investigate conformational changes during...
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