Researchers

Prof. Ryu investigates the structural dynamics of chromosome-organizing proteins and membrane proteins using High-Speed Atomic Force Microscopy (HS-AFM) together with single-molecule fluorescence and magnetic tweezers assays. By directly visualizing these molecules in action at nanometer and millisecond resolution, this work reveals the molecular mechanisms of chromosome organization and membrane signaling—processes whose dysregulation underlies many human diseases. An example is chromatin compaction and its link to cancer. We recently showed that a Q→R mutant of PRC2 drives aberrant chromatin compaction, providing a structural basis for how this mutation promotes thyroid carcinogenesis. We have also found that key chromosomal proteins such as cohesin undergo bridging-induced phase separation, and that oncogenic mutants alter this condensation behavior—an increasingly recognized driver of malignant transformation. On the membrane side, we directly visualized how endotoxin (LPS) is delivered to Toll-like receptor 4 (TLR4), capturing the dynamic steps of innate immune activation relevant to sepsis and inflammatory disease. Collectively, these approaches translate directly into medical relevance: elucidating disease mechanisms, enabling molecular-level diagnosis of pathogenic mutations, and identifying targets for drug development.