Xiaohan Li

Low resolution cryo-EM map that looks like Cuban's skull

When you still haven't solved the orientation bias of your protein sample #CryoEM

With Eugene Koonin, we propose a concept of “the selfish ribosome”, under which evolution of life is viewed as a ribosomal takeover, where the ribosome evolved to consume most of the cell’s resources, while other cellular componentry ensures the propagation of the ribosome. arxiv.org/abs/2602.23268

Job opening for Research Group Leader in Structural Studies at MRC Laboratory of Molecular Biology, focusing on macromolecular structures.

Are you a structural biologist pushing the boundaries of molecular science with an ambitious research programme?
Join our Structural Studies Division as a tenure-track Group Leader, with core funding, world-leading facilities & enthusiastic colleagues.
Apply by 16 MAR
www.nature.com/naturecareer...

Congratulations Alex! Been waiting for the in press version since the preprint — really exciting work!

Papers are like buses... You wait for ages, then two come along at once.

Huge congrats to @bornanovak.bsky.social and @jefflotthammer.bsky.social for pushing and driving every aspect of this work, preprinted ~1 year ago to the day (Friday before BPS), now published!

www.nature.com/articles/s41...

Structural basis of caveolin-driven membrane bending https://www.biorxiv.org/content/10.64898/2026.02.05.703862v1

As Fran was nice enough to highlight this, I thought I'd put up a brief thread. 3 in 10 proteins that our cells make are either embedded in membranes (ion channels, adhesion molecules, etc.) or secreted (insulin, antibodies). They move through the secretory pathway.
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Suyang Zhang smiles in front of a blurred laboratory background

Exciting opportunity for a #postdoc to join @suyangzhang.bsky.social’s group in the LMB Structural Studies Division to investigate co-transcriptional splicing using cryo-EM and biochemistry.
Read more: www.nature.com/naturecareer...
Apply by 11 FEB
#PostdocJobs #ScienceJobs

Why do mated songbirds sing beautifully coordinated duets? My Ph.D. work showed that duets are cooperative signals that pairs use to defend their shared territory. This visual summary is based on Logue & Gammon 2004 Animal Behaviour 68: 521-531 and Logue 2005 Cognition, Brain, Behavior 9:497-510.

Roadmap for Condensates in Cell Biology Biomolecular condensates govern essential cellular processes yet elude description by traditional equilibrium models. This roadmap, distilled from structured discussions at a workshop and reflecting t...

Physicists' perspective on the future direction of condensates in Cell Biology.
arxiv.org/abs/2601.03677

Knowledge is about interacting with nature, making reasoning, then communicating the excitements and discovery to the community; not by chewing “decoders” output and then throw random things to “encoders” and sell the outputs again.

Really don’t understand why loads of people are advocating delegation of paper reading and reference searching to AI, and even paper-writing using AI. It’s like volunteering to be left out of the discovery process and intellectual works, happily living as a slave to the “transformers”.

Experimental structures provide valuable hypotheses and accelerate but do not replace evolutionary and statistical analyses of protein sequences

Very exciting project! Trafficking, IDRs, and structural biology!

Apologies I was a bit unclear with "unstructured in functional complex"; I was suggesting the possibility of structured regions interact to provide specificity (frequently enthalpy contributions), IDRs remain unstructured to tune entropic effects of the system, keeping them dynamic.

Intrinsically disordered proteins drive membrane curvature - Nature Communications Proteins that bend membranes often contain curvature-promoting structural motifs such as wedges or crescent-shaped domains. Busch et al.report that intrinsically disordered domains can also drive memb...

For the "remain disordered in functional state", I tend to think most AF2 predicted low pLDDT regions belongs to this class, frequently doesn't involve in a binding event. One quick example in my head is the epsin/AP180 example www.nature.com/articles/nco...

I think one classic example of both disordered then to stable helical transition, might be the ACTR-CBP system. pubmed.ncbi.nlm.nih.gov/11823864/ pubmed.ncbi.nlm.nih.gov/24449148/

In this case we may also want to revisit the definition of IDRs and reclassify…we used to define them as no stable secondary/tertiary structures in solution, but this may simply be a reflection of good solvation. We may redefine “canonical IDRs” as being unstructured even in functional complexes

I guess in this case the only case of exception might be when two IDRs interact with each other they co-fold with each other which gives a specific new interface… but considering the amount of entropic penalty from IDR-IDR to complete structure, this might be rare…

This is a great point! In this case, would you think it might also be a good idea to treat IDR-IDR interaction differently than IDR-folded domain interaction, independent of the affinity? Maybe as long as one of the partner is folded, the interface would already be specified…

Postdoc opportunity with Michel Goedert and myself to work on #cryoEM/#cryoET structures of #amyloids. Feel free to email me with any questions you might have.

mrc.tal.net/vx/mobile-0/...

Hi Andrea, I really like your paper cited here. The figure highlights the importance of cellular context not just for phase separation studies, but for interpretation of most in vitro data involving interactions between macromolecules in general as well, especially for low affinity ones...

Our review on Integrative modelling of biomolecular dynamics 💃 is now live at COSB

We discuss approaches to integrate computational methods with time-dependent & time-resolved experiments to study protein dynamics

With @dariagusew.bsky.social & Carl G. Henning Hansen
doi.org/10.1016/j.sb...

I found a tiny octopus on the tide pool🐙✨️

Small as it is, it’s every bit an octopus ... and absolutely adorable!!

It even shoots ink🫧 ͛.*

I agree. I think protein folding is evidence that one can form specific structures that are thermodynamically driven by non-specific, dynamic interactions, with additional contributions to specificity from h-bonds etc (that probably contribute less to the "driving" force).

The structure of most folded proteins are stabilised by the hydrophobic effect which in some sense is quite fuzzy. And the hydrophobic cores of proteins can be quite dynamic.

Many congrats Shahar! Really beautiful work and great datasets to look at!

Protein surface chemistry encodes an adaptive tolerance to desiccation Desiccated cells lose over 85% of their water content and experience widespread biomolecular dysfunction. Romero-Pérez et al. show that the yeast proteome contains a subset of proteins that are desicc...

Now published in @cp-cellsystems.bsky.social - we look at the chemical features that make proteins tolerant to dehydration, and the functions these proteins fill. 🏜️🚱 tinyurl.com/bsfy56yt

yep, this is very concerning.

Some have already tried to raise the alarm in 2022, and since then, the “quality” of AI-generated images has only improved...

www.cell.com/patterns/ful...

Language models cannot reliably distinguish belief from knowledge and fact - Nature Machine Intelligence Suzgun et al. find that current large language models cannot reliably distinguish between belief, knowledge and fact, raising concerns for their use in healthcare, law and journalism, where such disti...

Language models cannot reliably distinguish belief from knowledge and fact #AI

Failure to make such distinctions can mislead diagnoses, distort judicial judgments and amplify misinformation.

www.nature.com/articles/s42...