G-quadruplexes often need to be unwounded in cells. We characterize this process by steered #moleculardynamics simulations with force loads small enough to be reached by modern experimental pulling techniques. The work is now out in @JCIM_JCTC: doi.org/10.1021/acs.jcim.3c0… @BFUavcr

The unfolding mechanism depends on the force direction, GQ topology, and the pulling speed (the slower the speed, the more complex the unfolding pathways).

In collaboration with @dmonchaud and Jun Zhou laboratories, we combined extensive theoretical and experimental approaches to reveal how DNA G-quadruplexes fine-tune their biocatalytic properties. #moleculardynamics

In cooperation with Jens Wohnert’s team from @goetheuni of Frankfurt, our colleagues at @BFUavcr used #moleculardynamics and #QM to elucidate structural basis for function of pseudouridine - the most widespread chemical modification in eukaryotic transcriptome. Out in @RNAJournal

What is the mechanism of #RNA-#protein binding? In our recent work, we visualize atomic pathways of single-stranded RNA binding to protein domains with unbiased MD simulations for the first time. Article available in @NAR_Open: doi.org/10.1093/nar/gkac1106 #moleculardynamics,#compchem

We study two RNA-protein complexes and show that RNA-protein binding is a multi-pathway process. A partially disordered pre-binding state is involved in one case. The work necessitated the development of a goal-specific force field modification to weaken RNA self-interactions.

what can #moleculardynamics tell us about the structural dynamics of (dis)ordered #RNA-#protein complexes and where are the limits? Our new study revealing structural ensembles of the RNA-bound FUS protein is out at @JPhysChem: doi.org/10.1021/acs.jpcb.2c0…