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Data · dataset · 2026

Data for: Boosting Sensitivity of High-Dimensional Solid-State NMR of Proteins by Optimizing Coherence Transfers

Listed in TUDOdata

Owing to fast magic-angle spinning, solid-state nuclear magnetic resonance has evolved as a versatile method to decipher protein structure, dynamics, and chemical properties.

Description

While higher-dimensional approaches such as 4D and 5D correlation spectra are generally capable of exceeding the established molecular-weight limitations by ameliorating signal overlap, their intrinsic implications for sensitivity and measurement times required have limited these important prospects till-date.

Here we show that the extensive use of dedicated transverse-mixing optimal control pulses (TROPs) in high-dimensional experiments to enable concomitant transfer of complex signals along consecutive magnetization transfers can reduce the necessary measurement time by an order of magnitude. Owing to the multiplicative benefits of the enhancement for successive indirect chemical-shift dimensions, combined with non-linear benefits upon spectral reconstruction, the combination of non-uniformly sampled, higher-dimensional approaches with pulse sequences derived from concatenated TROPs presents itself as transformative with regard to feasibility of in-depth NMR characterization and hardware requirements.

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The data publication includes data sets and processing scripts for the experiments presented in the publication. Every file contains at least the raw, i.e., sparse FID, all information stored by default in TopSpin, e.g., acqus files, as well as processing scripts used for data conversion and projections of the reconstructed spectra for every used algorithm. Some 4D data sets will additionally include the full spectrum processed by SSA, while for other, size limitations prevent the upload.

The 5D data sets contain projections as well as spectra in their 2D stacked version in files named x-sections.ucsf Please check README for more details!

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Chemistry
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