M. W. van der Kamp

The paper investigates how electric fields in class A β-lactamases influence carbapenemase activity using molecular dynamics simulations and identifies key positions that correlate with enzyme efficiency.

This study investigates the temperature dependence of enzyme catalysis by analyzing MalL and its mutants, showing cooperative conformational transitions and introducing models to explain non-Arrhenius behavior.

This study shows that epistasis in enzyme evolution arises from shifting the rate-limiting step in the catalytic cycle, leading to substantial activity enhancements through synergistic mutations.

This study develops protocols for reliable in silico ranking of TCR binding affinities using MMPBSA and MMGBSA methods, showing that short MD simulations can accurately evaluate TCR variants.

This study shows that increasing rigidity in a de novo peroxidase enhances its activity but alters its temperature dependence, resembling natural enzymes.

The paper shows that low β-lactam concentrations drive cryptic evolution of β-lactamases through fitness benefits in competition experiments, not increased resistance.

This study shows that directed evolution of a designer enzyme introduces dynamical changes that increase activation heat capacity and nonlinearity in temperature dependence through correlated dynamical networks.

The paper shows how the histidine kinase BceS of Bacillus subtilis is controlled by its cognate ABC-transporter to enable energy-efficient antibiotic resistance activation based on need.

The paper uses experiments and simulations to show that heat capacity changes in enzyme-catalyzed reactions can be predicted by molecular dynamics simulations, revealing dynamic changes beyond the active site.