Article ID Journal Published Year Pages File Type
1925564 Archives of Biochemistry and Biophysics 2012 6 Pages PDF
Abstract
► Metal-binding loop mutations in azurin reduce the protein thermal stability. ► The AZPC chimera has lower thermal stability compared to the AZAMI mutant. ► The thermal unfolding is irreversible and kinetically controlled. ► The length of the copper binding loop modulates the protein stability.
Keywords
Related Topics
Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
Preview
The influence of active site loop mutations on the thermal stability of azurin from Pseudomonas aeruginosa
Authors
, , , , , ,