Flexibility Correlation between Active Site Regions Is Conserved across Four AmpC β-Lactamase Enzymes
Fig 2
Physical descriptions of the original four AmpC structures.
Thermodynamic descriptions of the unfolding transition are characterized by (A) heat capacity and (B) the free energy landscapes. The vertical dashed line indicates the experimental Tm value of the E. coli enzyme. The experimental ΔHunf value is 182 kcal/mol, whereas the calculated value is 212 kcal/mol. (C) Rigid cluster susceptibility curves describe the mechanical transition for a structure predominantly composed of one large rigid cluster to many disjoint and floppy tiny clusters.