Structural reorganization renders enhanced metalloprotein stability.
نویسندگان
چکیده
The enhanced stability of a mesophilic metalloprotein was assessed using biophysical spectroscopies. Significant local structural interconversions 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.
منابع مشابه
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ورودعنوان ژورنال:
- Chemical communications
دوره 47 39 شماره
صفحات -
تاریخ انتشار 2011