Guillaume Stirnemann

This study uses molecular dynamics simulations to analyze the conformational ensembles of the hairpin ribozyme's active site along competing catalytic pathways, finding that monoanionic pathways are more favorable than a dianionic mechanism.

This paper reviews computational strategies for exploring RNA conformational ensembles, focusing on energy landscape-based approaches and atomistic simulations, and discusses challenges and future directions.

The paper shows that 2'-O-methylation alters ribozyme active site geometries and reaction mechanisms, challenging assumptions about its role in stabilizing pre-catalytic conformations.

This study uses high-pressure NMR and molecular dynamics simulations to reveal how a bacterial membrane protein, OmpX, interacts with lipid bilayers at the atomic level, showing how lipid dynamics influence protein structure and function.

This study uses molecular dynamics simulations to assess vinculin-actin unbinding kinetics, revealing catch bonding behavior under force and showing how directional forces influence bond states.