Ale Mongera

@mongeralab.bsky.social

Developmental biologist at UCL Multicellular Morphogenesis Lab http://zebrafishucl.org/mongera-lab

I won't pay $4,000 for a ticket to see my Knicks play in the NBA Finals for the first time in 27 years, but for some reason I routinely pay three times that much for open access to papers that I wrote myself.

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Massive congratulations to our Editor-in-Chief for being elected as a Fellow of the Royal Society @royalsociety.org. This is an incredible honour for our journal. @ucl.ac.uk @ucl-cdb.bsky.social

International Society of Developmental Biology@isdb.bsky.social · 2mo ago

‼️MASSIVE‼️ congratulations to Professor Roberto Mayor @mayorlab.bsky.social from UCL, who has been elected as a fellow of The Royal Society @royalsociety.org. Professor Mayor is a Professor of Developmental and Cellular Neurobiology and one of our board of directors. royalsociety.org/news/2026/05...

How much information does it take to fold a protein? Not much, if you use the right information! We find that residue burial, a binary label of core vs surface, encodes a protein's fold highly efficiently and even improves ESM2's structure representation. 1/8 www.biorxiv.org/content/10.6...

Residue burial encodes a protein's fold

Protein structure is controlled by a high-dimensional energy landscape, which is a function of all of the atomic coordinates of the protein. Can this landscape be accurately described by a low-dimensional representation? We find that residue core identity, a binary N-dimensional encoding indicating whether each of the N amino acids in a protein is buried in the core or not, can predict the protein's backbone conformation more efficiently than all other representations that we tested. Core identity is 4 times more efficient than previous estimates of the bits per residue needed to encode a protein's native fold, 2 times more efficient than the Cα contact map, and 1.5 times more efficient than the machine-learned embeddings from FoldSeek's 3Di. Even when the folded structure is unavailable, predicting each residue's burial from sequence yields a more accurate estimate of fold quality than predicting pairwise contacts from the same sequence information. Thus, this work emphasizes that the problem of determining a protein's native fold can be re-framed as predicting each residue's core identity. ### Competing Interest Statement The authors have declared no competing interest. Chan Zuckerberg Initiative (United States), 2023-329572 NIH, T32GM145452

biorxiv.org

🎉 The Developmental Mechanics Seminar Series is back! 🗓️ Thurs, Jan 22 🎙️ Opening talks: 🧬Guy Tanentzapf (UBC) — How cell adhesion molecules wire into the cytoskeleton 🌀Juan Manuel Gomez Elliff (EMBL) @gomezjm-devmech.bsky.social — Mapping tissue mechanics with Brillouin microscopy

International Developmental Mechanics Seminar Series

Please fill out the following survey if you are interested in the 2025-2026 International Zoom Seminars on Developmental Mechanics.

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