Evidence map›Paper›PMID 41915276›Full record

ArticleJournal of biomolecular NMR2026

Super-Resolution solid-state NMR Spectroscopy.

Olivia Gampp, Riccardo Cadalbert, Roland Riek, Sarah A Overall

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Olivia GamppInstitute of Molecular Physical Science, ETH Zürich, Vladimir-Prelog-Weg 2, Zürich, CH-8093, Switzerland.
Riccardo CadalbertInstitute of Molecular Physical Science, ETH Zürich, Vladimir-Prelog-Weg 2, Zürich, CH-8093, Switzerland.
Roland RiekInstitute of Molecular Physical Science, ETH Zürich, Vladimir-Prelog-Weg 2, Zürich, CH-8093, Switzerland. roland.riek@phys.chem.ethz.ch.
Sarah A OverallInstitute of Molecular Physical Science, ETH Zürich, Vladimir-Prelog-Weg 2, Zürich, CH-8093, Switzerland. soverall125@gmail.com.

Funding

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung 200021-228182
6 · The paper itself

Abstract

Solid-state NMR spectroscopy is often limited by low spectral resolution, a problem typically addressed using fast magic-angle spinning (MAS) and ¹H detection, which require costly specialized hardware. Here, we demonstrate that the super-resolution method-previously applied in solution-state NMR-can be successfully implemented in solid-state NMR to enhance resolution. Applying dynamic number of scans (DNS) sampling to 2D ¹³C-¹³C DARR experiments on the AP205 capsid protein yielded an effective doubling of resolution, halving peak widths from ~ 180 Hz to ~ 87 Hz. Furthermore, DNS acquisition provides a significant advantage over post-acquisition apodization of conventional data with a 20% gain in sensitivity, yielding 309 more detectable peaks with 20% more sequential contacts and 25% more long-range contacts. This method is simple to implement and provides a powerful, accessible strategy to greatly improve the quality of solid-state NMR spectra applicable at all MAS frequencies.

Indexed as

Capsid ProteinsNuclear Magnetic Resonance, BiomolecularCapsid Proteins

Identifiers

PMID41915276
PMCPMC13038466

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.