D. V. Laurents

The paper analyzes glycine-rich polyproline II helix assemblies to identify common structural features that could aid in protein design.

This study uses NMR spectroscopy to analyze the denatured state of snow flea antifreeze protein, revealing conformational entropy and structural insights into PPII helical bundle stability.

This study shows that FUS globular domains undergo cold denaturation, promoting phase separation under cold stress conditions.

This study shows that the SARS-CoV-2 Nsp8 N-terminal domain dimerizes and contains both folded and disordered regions.

The paper uses NMR spectroscopy to study the disordered C-terminal region of SARS-CoV-2 Nsp2, revealing partial structure and dynamic behavior.

The paper investigates whether Gly-rich segments of disordered proteins form polyproline II helices, which may contribute to biomolecular condensate stability.

This study uses AFM-SMFS to show that tau aggregation is associated with reduced conformational polymorphism, driven by mutations and chemical conditions.

This study identifies preferred conformations in the intrinsically disordered region of human CPEB3 using NMR spectroscopy, revealing structural motifs and potential functional interactions related to memory consolidation.

The paper shows Phe-Gly motifs drive fibrillization from TDP-43 droplets, revealing structural differences between droplets and fibrils.

The paper investigates cohesin-dockerin interactions in cellulosomes, revealing two binding modes and an allosteric regulation mechanism via proline isomerization.