We got a clue to my unsolved question from high school 🌱
“Chromatin loop organization insulates transcription”—a schematic I once scribbled in my textbook like this.
But ever since, I’ve wondered: How can neighboring loops avoid interacting?
(3/n)

And again, Fantastic meeting! 🔬
Single-molecule studies are advancing biology into new territory—thrilled to be involved. 💡
#EMBLSingleMolecule

I had an amazing time at EMBL Heidelberg!
I was absolutely impressed by the facilities—everything operates on a completely different scale here.
Definitely hope to work in an environment like this someday.

Honored to receive 1st Place Poster Award 🏆 at the EMBL meeting "Gene Regulation: One Molecule at a Time"!
Thank you to all who visited and engaged in exciting discussions.
Grateful to the organizers for an excellent event! #EMBLSingleMolecule

Huge thanks to Rosana @rcollepardo.bsky.social, Charlie, Jan @janhuemar.bsky.social, and Stephen! 🙌
Their simulations revealed in stunning detail how H1 and nucleosomes interact.
I was amazed—so consistent with our experiments! 🔬💻
(4/n)

Single molecule imaging revealed that H1 behaves like a liquid inside chromatin! 🫧
It's amazing to witness how H1 behaves in living cells 🔬✨
(3/n)

H1 is the most abundant chromatin protein, condensing chromatin—but how? 🤔
The textbook model suggests H1 stabilizes 30-nm fiber, but recent studies dispute this. So, what's the true mechanism?
We think: H1 acts as a liquid-like "glue"! (2/n)

My first, first author paper is now on bioRxiv! 🤩

Linker histone H1 is a liquid-like "glue" condensing chromatin, which revises textbooks! 📖✨
biorxiv.org/content/10.1...

Huge thanks to my PI, @kazu-maeshima.bsky.social, for supervision.
Amazing collab with @rcollepardo.bsky.social’s group!" (1/n)