SFB 1551 - Collaborative Research Centre 1551

@sfb1551.bsky.social

In this Collaborative Research Centre (Sonderforschungsbereich, SFB) life scientists and polymer scientists jointly study biomolecules as biopolymers with a focus on their polymeric nature.

📢 Coming up soon: Peptide Self-Assembly Conference 2026! Join the international supramolecular science community in Mainz, Germany, from 10–12 August 2026 for 3 days of cutting-edge research on peptide self-assembly, biomaterials, catalysis, sustainable chemistry, & more. www.psacon2026.com

PSA Conference 2026 - Peptide Self-Assembly Conference hosted in Mainz.

Following the success of the Pepetide Self-Assembly (PSA) Manchester meeting in 2023, we are excited to host PSA Conference 2026 in Mainz, on August 10-12th. The conference will take place on the prem...

psacon2026.com

Congratulations to Andreas Bock, from University Medical Center Mainz and associate member of the SFB1551, on being awarded the ERC Consolidator Grant for his project "CLARITY" on "Elucidating the Role of Subcellular GPCR Nanoswitches in Signaling Specificity" Well done!

European Research Council (ERC)@erc.europa.eu · 11mo ago

The results of the ERC Consolidator Grant call have been announced! 📣 349 researchers have been selected for funding. Congratulations to all! #ERCCogG! 👉 buff.ly/uu62uFV #FrontierResearch #EUfunded #HorizonEurope @scienceinnovation.ec.europa.eu

🖥️ New Publication Alert Congratulations to Eric Schumbera, @dormannlab.bsky.social, @waltherlab.bsky.social & @miguelandrade66.bsky.social on their recent publication in BMC Genomics #RGmotifs #IDRs #LLPS #HumanProteome #ComputationalMotifAnalysis bmcgenomics.biomedcentral.com/articles/10....

Computational investigation of the sequence context of arginine/glycine-rich motifs in the human proteome - BMC Genomics

Arginine-glycine (RG)-rich motifs are among the most prevalent RNA-binding elements within intrinsically disordered regions (IDRs) of proteins and play crucial roles in RNA metabolism, gene regulation, and the formation of membraneless organelles via liquid phase separation (LLPS). Despite their biological relevance and implication in neurological disorders and cancer, the sequence features and context dependencies that define functional RG motifs remain poorly characterized owing to their disordered nature and sequence variability. In this study, we present a computational framework to dissect the sequence and structural context of RG motifs across the human proteome. By contrasting a functionally defined positive dataset—enriched for RNA-binding and phase-separating proteins—with a negative dataset of RG motif proteins lacking these annotations, we identified distinct compositional and contextual signatures. RG motifs in the functionally defined positive dataset show increased enrichment of phenylalanine, tyrosine, aspartic acid, and asparagine, both within and around the motif, as well as nonrandom spatial relationships with structured RNA-binding domains. Notably, phenylalanine and tyrosine exhibit divergent positional and functional profiles, suggesting distinct mechanistic roles. Our analysis highlights the potential of sequence-based approaches to uncover functional determinants in disordered protein regions and further advances our understanding of the properties of RG motifs, offering a transferable framework for the study of other low-complexity motifs.

bmcgenomics.biomedcentral.com

✨ Polymers: The Hidden Heroes of Life ✨ Thrilled to share that our science outreach chapter has just been published in the Springer Series "Science for a Better Tomorrow"! A true example of how collaboration and curiosity can drive meaningful science communication! link.springer.com/book/10.1007...

Science for a Better Tomorrow

This book explores how biosciences, AI, and IT can innovate biomedicine and health, expanding on the discussion held at the Curious2024 Conference.

link.springer.com