ArticlebioRxiv : the preprint server for biology2026
AlphaFold reveals but sometimes distorts an organizational principle of protein folding.
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
12 authors.
Funding
Abstract
Proteins can adopt many distinct conformations, yet the sequence determinants governing which structural states are accessible remain poorly understood. Using fold-switching proteins and AlphaFold as an analytical lens, we identify an organizational principle in which access to alternative structural states-and in some cases the folded state-is governed by surprisingly few amino acids, termed gating residues. Gating generalizes to single-fold proteins, indicating that conformational accessibility is often hierarchically organized around a small number of disproportionately influential residues. AlphaFold has implicitly learned this principle but amplifies and sometimes misapplies it, concentrating conformational control onto too few or incorrect residues. Guided by this principle, targeted MSA editing recovered a conformation AlphaFold confidently mispredicted, suggesting a path toward more accurate prediction of alternative conformations and mutational effects.
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.