Daniel Friedrich

@friedrichlab.bsky.social

Research Group Leader and Head of #NMR Facility @chemunicologne.bsky.social‬ at @unicologne.bsky.social‬ | We are interested in structural analysis of proteins, peptides and nucleic acids. https://friedrichlab.uni-koeln.de/

Many thanks again for the great collaboration @gabriellapetti.bsky.social and @teamthomma.bsky.social!

Team Thomma@teamthomma.bsky.social · 2mo ago

📣Last week another @biorxivpreprint.bsky.social dropped: "A fungal pathogen effector that shapes host plant microbiota kills bacteria through lipoteichoic acid binding and membrane disruption" a joint effort by @nicksnelders.bsky.social & @gabriellapetti.bsky.social www.biorxiv.org/content/10.6...

Congratulations @gabriellapetti.bsky.social and @teamthomma.bsky.social on this fantastic study! It has been a pleasure collaborating with you, and we are very happy to have contributed with #NMR to such an exciting project. We truly enjoyed working together with you!

Gabriella Petti@gabriellapetti.bsky.social · 2mo ago

Excited to share our latest study with @nicksnelders.bsky.social and @teamthomma.bsky.social! We uncover the mode of action of the V. dahliae antimicrobial effector Ave1 and show that it binds LTA and disrupts bacterial membranes 🦠 www.biorxiv.org/cgi/content/...

@jacs.acspublications.org (open) Hyperpolarized NMR Reveals Low-Populated Folding Intermediates in DNA, Milan Zachrdla, Ertan Turhan, Michala Bučková, Robert Hänsel-Hertsch, Lukáš Trantírek* @ceitec.eu Dennis Kurzbach* @univie.ac.at pubs.acs.org/doi/10.1021/... #NMRchat 🧲

Hyperpolarized NMR Reveals Low-Populated Folding Intermediates in DNA

Nuclear magnetic resonance (NMR) spectroscopy is the only biophysical technique capable of characterizing nucleic acid structures at atomic resolution under near-physiological liquid-state conditions. Still, it is fundamentally limited by intrinsically low sensitivity, particularly when analyzing high-molecular-weight, low-abundance, or polymorphic targets, such as DNAs (DNA). In this study, we demonstrate that hyperpolarized aqueous buffers generated via dissolution dynamic nuclear polarization (dDNP) significantly enhance the 1H NMR signals of multiple DNA motifs. The resonances of labile imino and amino protons of DNAs dissolved in hyperpolarized buffers are enhanced up to ∼200-fold and ∼370-fold, respectively. These intense signals serve a 2-fold purpose: (i) as structural fingerprints of DNA folding topologies and (ii) they enable the direct observation of low-populated folding intermediates in DNA polymorphs, such as G-quadruplexes (G4) and i-motifs (iM), which remain undetectable by standard methods. Thus, our findings establish hyperpolarized NMR as a high-sensitivity method for probing DNA structures and folding intermediates across a wide range of motifs, opening possible avenues in liquid biopsy applications and cell-free DNA.

pubs.acs.org

Happy Thanksgiving! It’s been indeed a fantastic event and I’m grateful to join the inspiring Fulbright-Cottrell scholars and this great community. I’m looking forward to work together on innovative concepts in combining teaching and research!

guenther@thielelabs.bsky.social · 8mo ago

Great Thanksgiving 🦃 and networking 🕸️ event with an amazingly productive and creative Work-Brunch. Always fun to get together with the gang, and congrats to the new awardees @lisavondung.bsky.social @friedrichlab.bsky.social. with @hellmichgroup.bsky.social but missing @esteslab.bsky.social

Really interesting to see some basic science research coming out of Apple Inc. SimpleFold: Folding Proteins is Simpler than You Think arxiv.org/abs/2509.184... tldr: Apple used flow matching models to more efficiently predict protein folding structures. More of this, please... from ALL big tech.

SimpleFold: Folding Proteins is Simpler than You Think

Protein folding models have achieved groundbreaking results typically via a combination of integrating domain knowledge into the architectural blocks and training pipelines. Nonetheless, given the suc...

arxiv.org

Congratulations to the Behrmann and Schwarz labs at Institute of Biochemistry @chemunicologne.bsky.social for this fantastic work! 🎉 #StructuralBiology in Cologne is on fire 💥

Universität zu Köln@unicologne.bsky.social · 11mo ago

🧠 How Synapses Hold Together 🤝 This #discovery was made by a research team @bccologne.bsky.social studying the molecular architecture of #synapses. The study shows that the protein #gephrin forms flexible filaments in the brain, serving as an important building block of inhibitory synapses.

Molecular structure model of the gepherin protein complex on a gray background, with colored segments: yellow, blue, gray, red, and green, representing the protein subunits.

Exciting work from Duchardt-Ferner et al. in NAR: high-res. NMR structure of a tobramycin-responsive riboswitch. Shows a novel aminoglycoside-binding RNA motif with unique RNA-RNA contacts, explaining its exceptional switching efficiency in eukaryotic translation. academic.oup.com/nar/article/...

Structural basis for ligand recognition in the tobramycin riboswitch

Abstract. Recently, a novel tobramycin-responsive riboswitch was developed by a combination of Capture-SELEX and in vivo screening. This riboswitch regulat

academic.oup.com

New publication: Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme Our selective arginine labeling yields well-resolved 1H-detected spectra in solids (and solution). We apply it to study dynamics in crystalline ubiquitin and a >130 kDa large enzyme 1/2