This work is now officially published @natsmb.nature.com with some fun new analyses included in the revised version. Congratulations to all the authors! @connyyu.bsky.social @rappsilber.bsky.social @lrsinn.bsky.social @fjoreilly.bsky.social www.nature.com/articles/s41...

And it's now live in Nature Structural & Molecular Biology! Many thanks to James and @lapassmore.bsky.social for a great collaboration. www.nature.com/articles/s41...

A very late repost: Mad2 is an incredible metamorphic protein capable of adopting multiple conformations. Here we reviewed existing structural data and investigated this ever-changing protein using a combination of real-time NMR and MD simulations (kudos to Joe! @jgreener64.bsky.social)

🚨 New from PDBe! Check out the revamped PDBeChem service with enhanced Ligand Pages! 🔍 Explore detailed ligand data, interaction stats, bound structures, related ligands, and more—all in one place. 👉 Read more in the news: https://buff.ly/4g8eF6E

Happy to announce that the latest UniProt NAR paper is now out. Find out what we've been up to here academic.oup.com/nar/advance-...

In this work, James used NMR with @connyyu.bsky.social , crosslinking mass spec with the Rappsilber lab and biochemical reconstitution to discover that dispersed regions within the IDRs interact with multiple conserved binding sites on Ccr4-Not.

"You cannot by sheer force compel scientific truths to reveal themselves. The major insights come only to the individuals who have the patience to develop an intimate understanding of a problem, who have the space and the freedom to take professional risks and explore apparently bizarre ideas...