David Balchin

@davidbalchin.bsky.social

Group leader at the Francis Crick institute and head of the Protein Biogenesis lab. Interested in protein folding, ribosomes and molecular chaperones.

Out now in #NAR! 🧬 I mapped the evolution of the ribosomal exit tunnel through the "eyes" of the nascent chain using MD simulations. How do the tunnel geometry, lateral branching, and chemical landscape change across 64 distinct ribosomes from the 3 domains of life? academic.oup.com/nar/article/...

Evolution of the ribosomal exit tunnel through the eyes of the nascent chain

Abstract. The exit tunnel is a universally conserved feature of the ribosome that directs the nascent polypeptide into the cellular environment and is invo

academic.oup.com

We are looking for someone to lead the new Facility for Protein Biochemistry & Biophysics at the MPI of Immunobiology and Epigenetics in Freiburg — please spread the word and apply if you are interested!

Max Planck Institute of Immunobiology and Epigenetics@mpi-ie.bsky.social · last mo.

🚀 Job alert: We’re starting a new Facility – and you can lead it! The MPI-IE & @mariekeoudelaar.bsky.social are hiring a Head of Protein Biochemistry & Biophysics to launch and lead a brand-new Core Facility in Freiburg 🇩🇪. Once-in-lifetime-chance. Details ⬇️ jobs.ie-freiburg.mpg.de/jobposting/b...

Our new contribution about #ribosomes. While preparing computer simulations for another project, we noticed that many r-protein parts were missing from the #cryoEM model. Surprisingly, we found this to be a general feature: a coat of #IDPs on the ribosome's surface. www.biorxiv.org/content/10.6...

Ribosomes are covered by a coat of flexible protein fragments

Ribosomal proteins contain flexible terminal regions that are averaged out during electron density reconstructions, rendering them absent from experimental models derived by X-ray crystallography or c...

biorxiv.org

I suspect it's not widely known that (or how much) genetic variation that would otherwise be deleterious is "hidden" by buffering. Much of that is accomplished by a protein called Hsp90. I've written a feature for Nature about it. www.nature.com/articles/d41...

These ‘master’ proteins protect us from deadly mutations — and could inspire new drugs

Biology has clever ways to mask the effects of potentially harmful gene mutations. Scientists are investigating how this ‘buffering’ works — and how to exploit it.

nature.com

Postdoc opening with us at EPFL! Experimental project on how ATP driven chaperone cycles keep proteins out of equilibrium. We will quantify energy use, kinetics, and functional outcomes, including clients whose native-like functional state is stable only by sustained chaperone action.

Our recent investigation of the constriction in the bacterial ribosomal tunnel is online. Unbiased all-atom MD simulations of the entire ribosome and PDB analysis show, how flexible the constriction is. The flexibility is modulated by short nascent polypetides.

bioRxiv Biophysics@biorxiv-biophys.bsky.social · 5mo ago

Early nascent polypeptide dynamics are coupled to the flexibility of the ribosomal tunnel constriction https://www.biorxiv.org/content/10.64898/2026.03.10.710814v1

Please spread the word: the Structural Studies Division @mrclmb.bsky.social is looking for a new tenure-track, independent group leader with an exciting plan in any area of Structural (Molecular & Cell) biology, in discovery biology and/or methods development. 🥳 mrc.tal.net/vx/mobile-0/...

Research Group Leader Tenure Track - Structural Studies - LMB 2775 - Medical Research Council

Location: Cambridge. Vacancy: Research Group Leader Tenure Track - Structural Studies - LMB 2775. Closing Date: 16/03/2026, 23:55

mrc.tal.net

Join us at the @crick.ac.uk for the 2026 meeting of the UK proteostasis community! We especially encourage students and postdocs to attend and share their work. All talks (except the keynotes) will be selected from abstracts.

Proteostasis UK@proteostasisuk.bsky.social · 6mo ago

📣 UK Proteostasis Meeting 2026 – Registration Now Open! I’m delighted to share that registration is now open for the UK Proteostasis Meeting 2026, hosted by The Francis Crick Institute on 20–21 July 2026
. Please register here(lnkd.in/ervXMzWN) and through Eventbrite for payment (lnkd.in/eTxqjnQy)

I'm thrilled to share our new publication, with co-first author @ Niko Dalheimer, is now out on Nature. Check out how we use live cell single particle tracking to study real time dynamics between TRiC chaperonin system and it substrates in the crowded cellular environment.

Niko Dalheimer@niko-dalheimer.bsky.social · 6mo ago

I’m excited to share my first-author paper, with co-first author @rongqinxiaoxiao.bsky.social, now out in @nature.com. We developed a live-cell single-particle tracking platform to see how TRiC & prefoldin engage proteins during co- and post-translational folding. 1/9 www.nature.com/articles/s41...

New lab paper!! We develop a technology for real-time, single-molecule visualization of proteasomal substrate degradation in cells. We find that the site of substrate engagement by the proteasome determines decay kinetics, efficiency and co-factor requirement. www.biorxiv.org/content/10.6...

In vivo kinetics of protein degradation by individual proteasomes

Protein degradation by the proteasome is central to cellular homeostasis and has been studied extensively using biochemical and structural studies. Despite an in-depth understanding of core proteolytic activity, it has remained largely unresolved how individual proteasomes process substrates inside living cells where many substrate types and co-factors exist. Here, we establish a live-cell single-molecule imaging approach that enables direct visualization and quantification of protein degradation by individual proteasomes. Using this approach, we find that substrate identity, folding and protein-protein interaction have a surprisingly modest impact on processing efficiency, whereas the mode of substrate engagement greatly impacts substrate processing; degradation initiated from protein termini typically proceeds rapidly and with high processivity, whereas internal engagement constitutes a distinct processing mode that exhibits poor processivity and a specific requirement for the AAA+ family ATPase p97/VCP. Furthermore, degradation initiated from opposite termini proceeds with asymmetric rates in a sequence-dependent manner, demonstrating that directionality is an important feature of proteasomal processing in vivo. Notably, poly-glutamine substrates associated with neurodegenerative disease are efficiently degraded from one terminus but resist degradation when engaged from the opposite terminus, highlighting the importance of substrate engagement mode. Together, our results show that different modes of substrate engagement lead to different proteasomal processing outcomes in vivo and revise the prevailing view of the proteasome as a uniform degradation machine. ### Competing Interest Statement The authors have declared no competing interest.

biorxiv.org

Postdoc position available in my lab in Jena (Germany. jobs.leibniz-fli.de/jobposting/6... If you're interested in protein biochemistry of amyloid proteins and chaperones, this job may be for you. B2 Level German is required as the candidate will be involved in teaching in German.

Postdoc (m/f/x)

Our Research Group led by Janine Kirstein, Professorin at Friedrich-Schiller-University Jena, is looking for a highly motivated and talented Postdoctoral Researcher (m/f/x) to join a research project ...

jobs.leibniz-fli.de

I love AlphaFold—but please include PAE (Predicted Aligned Error) plots for every “interaction.” Pretty PDBs ≠ proof. If the PAE doesn’t show an interface, it ain’t one. Show the plots. Structural biology's reputation is on the line.