ArticlebioRxiv : the preprint server for biology2026
A detailed molecular picture of protein folding during active translation.
Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
All proteins can begin to fold on the ribosome, and many rely on co-translational folding to attain their native conformation. This process is not accounted for using structure prediction algorithms such as AlphaFold and its molecular details remain largely unknown. Here, we develop a hydrogen-deuterium pulse-labeling approach which reveals nascent polypeptide folding at a high level of structural detail and its kinetic coupling with translation. Two proteins exhibit hierarchical folding of structures smaller than a domain during translation. A third protein, however, does not have time to conformationally equilibrate on the ribosome, instead becoming kinetically trapped. This subsequently biases post-translational folding to avoid an aggregation-prone intermediate populated during refolding from denaturant. Our results reveal diverse strategies that promote robust protein folding during non-equilibrium translation.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.