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Membrane fusion between SARS-CoV-2 and host cells is mediated by the spike protein and involves the membrane-proximal external region (MPER), a trypto…

Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. SignificanceIn many cases accurate models of the low energy, most populated form of a protein’s three-dimensional structure can be rapidly determined using machine learning (ML) programs, such as AlphaFold. However, biomolecular function is often ...

Membrane fusion between SARS-CoV-2 and host cells is mediated by the spike protein and involves the membrane-proximal external region (MPER), a tryptophan-rich sequence implicated in viral entry. Here, we investigated the feasibility of MPER-derived ...

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...

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.

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...

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

Abstract. Deoxyguanosine quadruplexes (G4s) form stable non-B-DNA structures that can affect transcription, replication, and genome stability. Depending on

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....

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...

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

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.

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...

Using RFdiffusion, a general method for targeting intrinsically disordered proteins and regions for protein design has been developed.

The increase in antibacterial resistance is one of the greatest challenges in modern medicine, driving an urgent need to develop new drugs to combat resistant pathogens. Peptides represent a promising...

Abstract. Conference travel contributes to the climate footprint of academic research. Here, we provide a quantitative estimate of the carbon emissions associated with conference attendance by analyzi...