SecY paper online 2025-02-19 The collaborative study on SecY, together with Prof. Long LI's lab and Prof. Ning GAO's lab, has been published in Cell (Link). With experimentally resolved Cryo-EM structures, Yang conducted a series of molecular dynamics (MD) simulations to investigate how SecY influences the folding behaviors of the transmembrane substrates within SecY. The results demonstrated that the cytoplasmic and extracellular cavities of the SecY channel create two distinct environments, facilitating the unfolding and folding of the transmembrane segments, respectively. These results indicate that SecY is more than just a passive protein-conducting channel, it is a chaperone. Dali and Song also participated in the collaboration and conducted additional computations to validate the protein's function. Congratulations!
