ArticleChembiochem : a European journal of chemical biology2026
Comprehensive Biophysical Profiling Evidences Self-Oligomerization of Bacterially Expressed Pc Protein.
Article in Chembiochem : a European journal of chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Comprehensive Biophysical Profiling Evidences Self-Oligomerization of Bacterially Expressed Pc Protein.Chembiochem : a European journal of chemical biology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Polycomb (Pc) protein is a core component of Polycomb Repressive Complex 1 (PRC1) and plays a central role in epigenetic gene silencing, particularly during embryo development. Despite extensive functional characterization, structural understanding of Pc remains limited due to its intrinsic disorder, low sequence complexity, and propensity for dynamic self-association. Here, we report the recombinant production, purification, and biophysical characterization of Drosophila melanogaster Pc constructs optimized for structural studies. Using solubility-enhancing fusion strategies, we obtained milligram quantities of stable MBP-tagged Pc protein suitable for downstream analyses. Sequence-based disorder prediction, circular dichroism, and solution-based techniques indicate that Pc is predominantly intrinsically disordered outside its conserved chromodomain, whereas it retains a defined secondary structure upon fusion and oligomerization. Thermal shift assays, Nano-Differential Scanning Fluorimetry (nanoDSF), dynamic light scattering (DLS), and Size exclusion chromatography coupled to multi-angle light scattering (SEC-MALS) demonstrate strong buffer-dependent stability and concentration-dependent self-association into higher-order assemblies. Cryo-electron microscopy reveals pronounced conformational and oligomeric heterogeneity, which can be partially stabilized by gradient fixation. Complementary AlphaFold-based modeling supports a conditional folding mechanism in which Pc adopts more ordered architectures upon self-association. Together, our results establish a robust framework for the biophysical investigation of Pc protein and provide mechanistic insight into how intrinsic disorder, oligomerization, and self-association may contribute to Polycomb-mediated chromatin regulation.
Indexed as
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.