나노 바이오 동역학 연구실

Proteins must fold into precise three-dimensional shapes to work, and how they do so is one of the deepest questions in life sciences. For membrane proteins it is even harder: folding happens inside the oily, crowded environment of a cell membrane, a world we still understand poorly and one that AI structure prediction cannot yet explain. These proteins account for the majority of drug targets, so understanding how they fold matters not only for basic science but for medicine. We watch single molecules fold in real time, one at a time, to uncover rules that averaged measurements can never reveal. In a living cell, membrane proteins almost never fold alone. Helper proteins called chaperones guide them, and when this guidance fails, misfolding and disease can follow. Yet how chaperones actually work has been remarkably hard to see, because it means catching a helper and its client in the act. This is where our single-molecule tools open a door that other methods cannot. Understanding how the cell actively shapes folding, rather than leaving it to chance, is a frontier that connects protein folding to quality control, aging, and disease. Proteins rarely act in isolation. Many must find and bind their partners inside the membrane to carry out their jobs, from sensing signals to transporting molecules. How these partnerships form has long been treated as a simple on/off event, but the real process is far richer and mostly hidden from view. We developed a way to take a single protein pair apart and watch it come back together, step by step, inside a membrane. Revealing how molecular partnerships assemble helps explain how cells build the machinery of life, and how that machinery goes wrong in disease. Experiments show us what a molecule does; simulations help us understand wh