Daniel Friedrich

Congratulations again @gabriellapetti.bsky.social and @teamthomma.bsky.social! It was indeed a fantastic defence and you did an incredible job in utilizing and mastering NMR, Gabriella (among all the other things you achieved in your PhD)!

A dynamic displacement mechanism drives protein import into mitochondria Most mitochondrial proteins are produced in the cytosol and imported through the translocase of the outer mitochondrial membrane (TOM) to reach their final destination. Although this protein entry gat...

📢 New preprint alert!
How do proteins enter mitochondria? We uncovered a surprising mechanism at the mitochondrial entry gate—using #NMR, in vivo single-particle tracking, yeast experiments, and MD simulations to crack the code.
www.biorxiv.org/content/10.6...
#StructuralBiology #Mitochondria
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#EMA_award 🎖️ Nominations wanted for the 2026 #EMA Young Scientist Award by January 31, 2026!

The Young Scientist Award is awarded annually to a young scientist for work in the field of magnetism, mainly carried out in Europe.

All details and nomination forms are available here buff.ly/M2ADnNe

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.

@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 🧲

@instruct-eric.bsky.social webinar: Structure Meets Function!

Explore the power of #NMR spectroscopy and its impactful applications in #structuralbiology, #drugdiscovery, and #metabolomics here at CERM/CIRMMP!

Register now! events.teams.microsoft.com/event/d9ac1b...

Integrative In Silico and In Vitro Screening of Low Molecular Weight Compounds Targeting SARS‐CoV‐2 RNA Elements A combined virtual and nuclear magnetic resonance (NMR)-based screening approach identifies small molecules that bind conserved SARS-CoV-2 RNA structures. Diverse compound libraries are screened usin...

New publication alert 🎉
Our latest paper explores how small molecules can bind SARS-CoV-2 RNA, combining in silico screening with NMR experiments to uncover promising RNA-targeting candidates.

full text: chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/...

#RNA #NMR #screening #drugtargeting

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!

#research #hydrogenbonding

NMR spectroscopy studies of hydrogen bonding
(Dračínský) – Coord. Chem. Rev.: doi.org/10.1016/j.cc...

@iocbprague.bsky.social @czechacademy.bsky.social

DFT calculations and theory do not support enantiospecificity in NMR J-coupling constants - Nature Communications Nature Communications - DFT calculations and theory do not support enantiospecificity in NMR J-coupling constants

Josef Zwanziger, @aaronrossini.bsky.social, and I published a rebuttal of a recent Nature Commun. paper claiming that enantiomers produce large differences in J coupling constants.

doi.org/10.1038/s414...

Very nice article from @lek-lab.bsky.social including @roesslph.bsky.social, A. Sever and R. Ahmed, enjoyed reading it! #NMR

Fantastic opportunity to work on exciting projects with a great team @etzkornlab.bsky.social!

The Zuo1 C-terminal domain stabilizes DNA guanosine quadruplex (G4) structures located on Chromosome IX in Saccharomyces cerevisiae Abstract. Deoxyguanosine quadruplexes (G4s) form stable non-B-DNA structures that can affect transcription, replication, and genome stability. Depending on

Our work on DNA G4 interactions with Zuo1 in collaboration with @paeschkelab.bsky.social and the Penedo lab is out in @narjournal.bsky.social 😍

Full text: academic.oup.com/nar/article/...

#G4 #G-Quadruplex #NMR #smFRET #ChIP-qPCR

📢 Open Call! The Max Perutz Labs invite applications for a Full Professorship in Integrative Structure Biology with a focus on in situ structural biology using cryo-electron tomography (cryo-ET) and related methods. More details ➡️ tinyurl.com/brswbymu

We have progressed from data collection to data analysis.

Congratulations @lisavondung.bsky.social!!! 🎉👏

Synthesis of Selectively 13C/2H/15N‐ Labeled Arginine to Probe Protein Conformation and Interaction by NMR Spectroscopy We offer a new labeling approach to introduce isolated 15N−13C−1H spin systems to the side chains of arginine residues. The labeling scheme delivers high-resolution NMR spectra to study large protein....

Darja combines organic-chemistry synthesis (with our great collaborator Roman Lichtenecker) of specifically isotope-labeled amino acids with protein NMR in solution and solids.
👉 Synthesis and proof of principle is here: chemistry-europe.onlinelibrary.wiley.com/doi/full/10....

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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...

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.

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

Huge congratulations again @kathlab.bsky.social ! 👏 So much deserved and we are incredibly glad to have you @chemunicologne.bsky.social! 🍾🎉

I enjoyed the talk by Harald Schwalbe @schwalbe-lab.bsky.social very much, especially the #NMR work on #RNA structure and dynamics! #FGMR #GDCh

Postdoctoral position in viral protein NMR, Prof Anja Böckmann, The protein solid-state NMR laboratory within the Molecular Microbiology and Structural Biochemistry (MMSB) unit in the Lyon Gerland Bioscience Campus mmsb.cnrs.fr/en/

emploi.cnrs.fr/Offres/CDD/U... #NMRjobs #NMRchat 🧲

Very nice work by the Wöhnert group, determining an intersting RNA structure using #NMR!

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

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/...

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

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Very interesting #NMR work on disordered proteins by the lab of @millessigrid.bsky.social at @fmp-berlin.de! Enjoyed reading it, congrats to this study!

📣 Massively proud of this ⬇️ great study, led by the brilliant @mesny.bsky.social surprisingly uncovering that many pathogen effectors stem from ancient antimicrobials 🤯 #EffectorWisdom #EvoMPMI

I‘m already looking forward to join this very interesting #NMR symposium and to meet friends from the good old times at @fmp-berlin.de! It’s still time to register!

Such a beautiful cover for @jacs.acspublications.org designed by @barthvanrossum.bsky.social! Nice #NMR work by the Lange lab at @fmp-berlin.de!

Intrastrand Peptide Staples That Promote β-Sheet Folding, Self-Assembly, and Amyloid Seeding Side chain stapling of cysteine (Cys) residues offers convenient entry into constrained peptides with enhanced bioactivity and bioavailability. Despite its widespread application in the constraint of α-helical, PPII, and loop conformations, the stabilization of β-sheet folds via intrastrand side chain Cys stapling remains largely unexplored. Here, we demonstrate that i→i+2 stapling with E-butenyl, butynyl, and m-xylyl linkers significantly enhances the folded population of two distinct β-hairpin model peptides. High-resolution NMR structures reveal that these staples support canonical β-sheet backbone torsions and stabilize cross-strand interactions. Leveraging the maintenance of intact backbone hydrogen-bonding edges, we employed i→i+2 side chain macrocyclization in the design of constrained β-arch peptides derived from the tau protein. We show that intrastrand stapling of a nonaggregation-prone segment promotes self-assembly into β-sheet-like filaments. The resulting filaments also seed the aggregation of endogenous tau in a cell-based assay in a macrocycle- and sequence-dependent manner. These findings establish di-Cys i→i+2 stapling as a versatile and synthetically accessible method to stabilize β-sheet structure and modulate the self-assembly of seed-competent amyloidogenic peptides.

Great work involving #NMR by @delvallelab.bsky.social in @jacs.acspublications.org on intrastrand side chain stapling of peptides, very interesting read!
pubs.acs.org/doi/10.1021/...

High-quality peptide evidence for annotating non-canonical open reading frames as human proteins A major scientific drive is to characterize the protein-coding genome as it provides the primary basis for the study of human health. But the fundamental question remains: what has been missed in prio...

The complexity of new functionalities enabled by thousands of non-canonical open reading frames potentially coding for miniproteins is just fascinating! I can see a lot of interesting #NMR studies on structure and function of #peptides

www.biorxiv.org/content/10.1...