Jobst Liebau

The paper investigates how electrostatic interactions control conformational changes and proton translocation in Complex I using a combination of experimental and computational methods.

The paper demonstrates functional dynamics in the eukaryotic RNA exosome using NMR and EPR, showing subunit flexibility and conformational changes in the Exo9 complex.

This study shows that buried ion-pairs in artificial proteins reshape folding pathways by introducing kinetic barriers that are overcome by hydrophobic collapse and core packing.

This study uses NMR to measure nanosecond methyl dynamics in the RNA exosome core, showing that relaxation-violated coherence transfer experiments can quantify side chain order parameters in large protein complexes.

The paper uses NMR and simulations to study dynamic motions in the eukaryotic RNA exosome complex, revealing conformational changes and a flexible plug region that blocks RNA pathways.