Thanks for the support of ITQB NOVA, the LS4FUTURE Associate Laboratory and the ITQB NOVA COVID task force. Congrats to all authors — Guillem Hernandez Gras, Maria Lança Martins, Nuno P. Fernandes, Tiago Veloso, João Lopes — extra proud that the whole crew behind this study hailed from ITQB NOVA!

By blending small-angle X-ray scattering, high-field NMR spectroscopy, computational modelling, molecular dynamics simulations, microscopy and fluorescence assays, we mapped these shape-shifting ensembles and showed how disrupting this coiled-coil interactions weakens droplet formation.

We found that a small “velcro-like” segment in the SARS-CoV-2 Nucleocapsid protein snaps identical proteins together, through coiled-coil interactions, building larger assemblies and liquid-like droplets that the virus relies on to wrap up its RNA.

setting up the production server. Collaboration between the Cordeiro lab at @itqbnova.bsky.social the @maciaslab.bsky.social at @irbbarcelona.org , António M. Baptista lab at @itqbnova.bsky.social and the Pau Bernadó lab at Centre de Biologie Structurale (4/4)

some #HTML for the general layout. Check the online version: kdsaxs.itqb.unl.pt . We have also open-sourced the code: lnkd.in/gN8bQR-9. You can also check our preprint: papers.ssrn.com/sol3/papers..... Many thanks to @itqbnova.bsky.social IT department for helping in (3/5)

a clearer view of protein equilibria and oligomeric states. In many labs, SAXS data can feel overwhelming - especially when proteins exist in several forms at once. This is where KdSAXS steps in. I had fun building KdSAXS mainly in #Python using #Dash with (2/5)