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Ferritin, comprised of 24 subunits, serves as a crucial iron storage protein, existing in two forms: apo (iron-free) and holo (iron-bound). Understanding the conformational changes and dynamic behaviour of single ferritin proteins in their native, unmodified state is essential for unravelling the functions of ferritin in various biological contexts. Currently, conventional single-molecule techniques like fluorescence resonance energy transfer and cryo-EM face challenges in tracking the small domain movements of proteins (Miller, et al., Rep. Prog. Phys, 2017). Such techniques require modifications of proteins that compromise the native protein state. As a result, the kinetic behaviour of ferritin in response to diverse buffer conditions and its pore-channel dynamics remain largely unexplored at the single-molecule level. Here, we demonstrate that optical nanotweezer using a gold double nanohole (DNH) can create localised …