단백질 스핀 동역학 연구실

Not all proteins have a well-defined structure. In fact, half of all mammalian proteins are either completely or partially disordered. However, the molecular details of these intrinsically disordered proteins (IDPs) are far less explored than those of well-ordered proteins, mainly because the tools to investigate IDPs are not well established. We study IDPs involved in neurogenerative diseases and focus on the flexible regions of membrane proteins, whose importance is often neglected in structural biology. Furthermore, we develop NMR methods to accurately characterize IDPs in solution. Imagine watching a high-resolution movie of cellular processes in live cells. We aim to investigate the structure and dynamics of proteins in live mammalian cells at atomic resolution. Solution NMR provides a unique opportunity to perform real-time structural biology in a physiological context, to gain a deeper mechanistic understanding of cell function and disease. In addition, we are also developing NMR pulse sequences, which are collections of magnetic-field pulses that control the quantum state of nuclear spins. The newly developed pulse sequences help investigate new aspects of biomolecules at high accuracy.