Associated Papers
Network of epistatic interactions in an enzyme active site revealed by large-scale deep mutational scanning.
Judge A et al.
Proceedings of the National Academy of Sciences of the United States of America, 2024
A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis.
Stojanoski V et al.
The Journal of Biological Chemistry, 2015
Structure of the wild-type TEM-1 beta-lactamase at 1.55 A and the mutant enzyme Ser70Ala at 2.1 A suggest the mode of noncovalent catalysis for the mutant enzyme.
Stec B et al.
Acta Crystallographica. Section D, Biological Crystallography, 2005
Select a paper to view details