Article
TEM-1 beta-lactamase folds in a nonhierarchical manner with transient non-native interactions involving the C-terminal region.
Biochemistry - 29 Jan 2008
Lejeune Annabelle, Pain Roger H, Charlier Paulette, Frère Jean-Marie, Matagne André
Abstract excerpt
The conformational stability and kinetics of refolding and unfolding of the W290F mutant of TEM-1 beta-lactamase have been determined as a function of guanidinium chloride concentration. The activity and spectroscopic properties of the mutant enzyme did not differ significantly from those of the wild type, indicating that the mutation has only a very limited effect on the structure of the protein. The stability...
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