Conformational changes in proteins, among the most abundant biomolecules in living systems, are fundamental to their function and are triggered by a variety of biological stimuli. A molecular-level understanding of these dynamic transitions is crucial for uncovering the mechanisms of diseases linked to protein dysfunction and for designing effective therapeutic strategies. These conformational transitions typically occur on timescales ranging from tens of microseconds to milliseconds, making them challenging to capture using conventional molecular dynamics (MD) simulations. While MD has been widely employed to study protein folding and free energy landscapes, the specific case of membrane-assisted protein conformational transition, which is central to my research, remains underexplored. In my previous work, I developed a finite-temperature string method to resolve atomistic transition pathways with high precision. Currently, my focus is on developing a coarse-grained multiscale simulation approach to explore large-scale conformational transitions in viral proteins, aiming to bridge the spatiotemporal gap between accessible computational scales and biologically relevant dynamics.</p>

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