We are excited to share our latest research published in Science Advances, titled “Influence of point mutations on PR65 conformational adaptability: Insights from molecular simulations and nanoaperture optical tweezers.” This study investigates how point mutations in the PR65 scaffold subunit of PP2A affect its conformational dynamics, leveraging in silico saturation mutagenesis, molecular dynamics simulations, and single-molecule nanoaperture optical tweezers. Our findings reveal how specific hinge-site mutations influence the protein’s structural flexibility, with implications for its regulatory functions.

Citation
Banerjee, A., Mathew, S., Naqvi, M. M., Yilmaz, S. Z., Zacharopoulou, M., Doruker, P., Kumita, J. R., Yang, S., Gur, M., Itzhaki, L. S., Gordon, R., Bahar, I. (2024) Influence of point mutations on PR65 conformational adaptability: Insights from molecular simulations and nanoaperture optical tweezer, Science Advances, 10, eadn2208 (Lead, Corresponding author) (IF10+,5-year IF: 13.8, IF:11.7)

View the publication
https://www.science.org/doi/10.1126/sciadv.adn2208