M. de Boer

This study evaluates the reliability and accuracy of single-molecule FRET for measuring protein structural dynamics and distances, finding high precision and accuracy with specific uncertainty limits.

This study finds increased sleep spindle activity in PTSD patients, correlating with intrusive memory symptoms, and introduces a new spindle detection method.

The paper shows that altering the stability of ligand-bound conformations can change ligand affinity in maltose-binding protein, beyond modifying binding site residues.

This study investigates the conformational changes in the sialic acid TRAP transporter SBP VcSiaP upon substrate binding, showing that substrate induces closure and provides structural insights for inhibitor development.

The paper investigates how structural dynamics in bilobed proteins evolve, showing that modifications to the structural core enable functional diversification through altered interdomain interactions and substrate specificity.

This study uses smFRET to analyze conformational dynamics of OpuA, an ABC importer, revealing ligand-binding mechanisms and ATP/glycine betaine dependencies.

The paper uses statistical mechanics to show that ligand-free and ligand-bound proteins can form the same conformations, and that changes in ligand-free conformational equilibrium affect ligand affinity.

This study identifies distinct EEG spectral changes in PTSD patients during NREM and REM sleep, correlating with insomnia and nightmares, and proposes a spectral index as a potential biomarker.

This study investigates how substrate-binding proteins (SBPs) in ABC importers change conformation and dynamics in response to different ligands, revealing that transport specificity arises from conformational plasticity rather than a unique closed conformation.