Solution-state NMR articles from across Nature Portfolio

DDX3X is a member of the RNA helicase family, which remodels RNA structures. Using solution NMR, here the authors show that DDX3X preferentially binds to single-stranded RNA, which underlies its unwinding activity toward various structured RNA substrates.

Import of proteins into peroxisomes depends on PEX5, PEX13 and PEX14. Here the authors obtain crystal structures and NMR data to show the recognition of diaromatic peptide motifs on a noncanonical surface of the PEX13 SH3 domain, revealing a dynamic network which modulates peroxisomal matrix import.

Binding modes of antigenically drifted hemagglutinins of human influenza A viruses have been determined by NMR using synthetic N-glycans having ¹³C-labeled monosaccharides to pinpoint which monosaccharides of extended LacNAc chains engage with the HAs.

Nuclear magnetic resonance (NMR) is a phenomenon at the heart of very important tools in analytical chemistry and medical diagnostics. Thirty-five years ago, Clifford Russell Bowers and Daniel Weitekamp developed the PASADENA experiment — an ingenious chemical scheme that boosts sensitivity of proton NMR by three orders of magnitude, widening the applicability of NMR altogether.

A strategy using pressure was devised to structurally identify conformational transitions in protein ensembles, allowing the rational prediction of mutations that induce pressure-driven enzyme activation. These results highlight the power of flexibility–function analyses in protein engineering design and applications.

A spin-jock’s path to biomolecular dynamics with NMR, and why solitude matters.