CD, solution NMR, Chemical Probing and EMSA raw data: core and extended ROQ with ADE RNA wt and derivatives

Local RNA structure is decisive for specific engagement with gene-regulatory proteins and, as a consequence, correct cellular function. However, its structure is often dynamic and, thus, challenging to study. Here, we show NMR and single-molecule force spectroscopy efficiently complement each other to provide high-resolution, time-resolved data on RNA folding intermediates during dynamic complex formation with the immune-regulating protein Roquin, which exploits multiple RNA-binding sites. Our data reveal a dual-mode binding of Roquin to RNA by firmly attaching to the stem-loop and, at the same time, destabilizing other regions, making them accessible to downstream interaction partners.The Excel dataset contains CD melting curve raw data for ADE RNA and bound Roquin proteins. The NMR zip folder contains raw and relevant processed data for core and ext ROQ with ADE RNA derivaties, ADE temperature series, ADE halves' NMR data, ADE mirrored data, and HNNCOSY data for ADE alone and with coreROQ. The EMSAs excel files contains all quantified and normalized bands for titrations, utilizable for fitting. The chemical probing data contain greyscale values for the ADR RNA alone and together with core and ext ROQ domains, as well as the alkalic ladder.All datasets are for: Tants, Walbrun et al., <i>Roquin exhibits opposing effects on RNA stem-loop stability through its two ROQ domain binding sites.</i> PNAS, 2025.See also related dataset specifically for SMFS data (optical tweezers) from this study: https://doi.org/10.6084/m9.figshare.28690193.v1