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 language | Unknown |
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Pages (from-to) | 11149-11151 |
Journal | Chemical Communications |
Volume | 47 |
Issue number | 39 |
DOIs | |
Publication status | Published - 1 Jan 2011 |