Andreas Walther

@waltherlab.bsky.social

Professor in Mainz/GER for Life-Like Systems and Materials, Max Planck Fellow, Travel and Food Enthusiast 🧳, AvHumboldt Postdoc-Scout 📧 me https://www.walther-group.com

👏👏👏Congratulations to SFB 1551 group leaders Edward Lemke @lemkelab.bsky.social and Andreas Walther @waltherlab.bsky.social at Johannes Gutenberg University Mainz (JGU) @unimainz.bsky.social @imbmainz.bsky.social on being awarded prestigious European Research Council (ERC) Advanced Grants.

Johannes Gutenberg-Universität Mainz@unimainz.bsky.social · last mo.

#ERCAdG für zwei Forschende der #UniMainz: Biophysiker Edward Lemke und Chemiker Andreas Walther erhalten Förderung in Millionenhöhe von der EU 👉 presse.uni-mainz.de/erc-advanced-… #ERCAdvancedGrant #Biophysik #Biomaterialien @imbmainz.bsky.social #ERC @erc.europa.eu @waltherlab.bsky.social

Auf der linken Seite des Bildes ist Prof. Dr. Edward Lemke zu sehen. Er ist Professor für Synthetische Biophysik an der Uni Mainz. (Foto/©: Thomas Hartmann / IMB)
Auf der rechten Seite ist Prof. Dr. Andreas Walther abgebildet. Er ist Professor für Makromolekulare Materialien und Systeme an der Uni Mainz. (© Andreas Walther)

I will soon be in Singapore (22-31.Jan) for the Dean's Distinguished Speaker Series #NTU #Singapore hosted by Ali Miserez. Very excited to go and thank you to Ali! @Singaporean researchers, if you want to meet me, I am happy to do so. PLease send me a direct message.

🖥️ 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