Michal H. Kolář

This study compares how different cationic chemistries influence peptide-RNA coacervation, showing that statistical peptide ensembles can drive protoribosomal condensate formation without sequence-specific optimization.

The paper identifies flexible protein fragments on ribosomes that are structurally invisible in experimental models and shows their compositional and functional significance across different ribosome classes.

This paper investigates the role of ribosomal peptides in protoribosome compartmentalization and stability, showing that RNA-protein interactions protect RNA from degradation and influence structural flexibility.