Sua Myong
Boston Children’s Hospital

Editor, Genome Biophysics and
Nucleic Acids
Biophysical Journal

What are you currently working on that excites you?

I’m fascinated by two interconnected phenomena. The first is how disordered protein molecules, at high concentrations, transition into liquid-like droplets known as “condensates”—micron-scale molecular gatherings with fluid properties. When these condensates lose their liquid-like nature and shift to gel or solid-like states, they can trigger toxic protein aggregation, fueling devastating neurodegenerative diseases. We recently uncovered that these molecules assemble into nanoscale particles, called “nanoclusters,” before merging into condensates. By capturing individual nanoclusters on our imaging surface, we precisely measured their size and material properties, offering a new window into this process. Second, the same disordered protein binds RNA co-transcriptionally—an interaction that we analyzed by using a newly implemented single-molecule assay. Strikingly, disease-linked mutants of this protein exhibit defective RNA binding, diverging from the wild-type behavior. This malfunction at the molecular scale may help explain the pathogenic mechanism behind neurodegeneration.

At a cocktail party of non-scientists, how would you explain what you do?

I’m a single-molecule biophysicist, which means I study how tiny molecules—like DNA, RNA, and proteins—move and interact in real time. To explain what I do, I sometimes bend, twist, or even dance to mimic their dynamic motions! Picture cars zipping down a highway, animals crossing a road, or birds landing briefly before taking off again—that’s how molecules behave. Because my research focuses on disease-related proteins, I compare healthy molecules to mutant ones, helping uncover how molecular malfunctions drive diseases. Many illnesses without treatments stem from unknown molecular causes, so understanding these tiny movements can unlock new paths for drug discovery—just like it did for HIV!