Structural reorganization renders enhanced metalloprotein stability

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Abstract

The enhanced stability of a mesophilic metalloprotein was assessed using biophysical spectroscopies. Significant local structural inter-conversions during thermal insult account for a reorganization of the protein scaffold, without disturbing the active metal site. This cushioning mechanism is proposed to be a generic property of metalloproteins contributing to enhanced stability.
Original languageUnknown
Pages (from-to)11149-11151
JournalChemical Communications
Volume47
Issue number39
DOIs
Publication statusPublished - 1 Jan 2011

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