Evidence map›Paper›PMID 42277067›Full record

ArticleScientific data2026

Complete NMR assignment for 275 of the most common dipeptides in intrinsically disordered proteins.

Tobias Rindfleisch, Emilie Fjeldberg Taule, Markus S Miettinen, Jarl Underhaug

Abstract readDataset
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific data, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

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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

2 citing papers in PubMed.

  1. Article
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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.

Tobias RindfleischComputational Biology Unit, Department of Informatics, University of Bergen, 5008, Bergen, Norway. tobias.rindfleisch@uib.no.
Emilie Fjeldberg TauleDepartment of Chemistry, University of Bergen, 5007, Bergen, Norway.
Markus S Miettinen *Computational Biology Unit, Department of Informatics, University of Bergen, 5008, Bergen, Norway. markus.miettinen@iki.fi.
Jarl Underhaug *Department of Chemistry, University of Bergen, 5007, Bergen, Norway. jarl.underhaug@uib.no.

Funding

Bergen Research Foundation BFS-NMR-1Research Council of Norway through the Norwegian NMR Platform, NNP 226244Sparebankstiftinga Sogn og Fjordane 509-42/16Trond Mohn Foundation BFS2017TMT01
6 · The paper itself

Abstract

Accurate NMR chemical shift assignments are essential for atomic-resolution characterization of proteins. Especially for intrinsically disordered proteins (IDPs) and regions (IDRs), however, the assignment remains a labor-intensive task due to spectral overlap and conformational heterogeneity. Consequently, complete side-chain assignments are rare. Here, we present a comprehensive reference dataset, comprising the complete NMR chemical shift assignments for 275 of the most prevalent dipeptides in the IDPome, covering 93% of it. In addition, we report side-chain protonation-dependent chemical shifts for dipeptides containing aspartic or glutamic acid. The dataset contains all NMR-accessible backbone and side-chain nuclei, in total 11 571 validated data points, as well as the 1D (

Indexed as

DipeptidesIntrinsically Disordered ProteinsNuclear Magnetic Resonance, BiomolecularDipeptidesIntrinsically Disordered Proteins

Identifiers

PMID42277067
PMCPMC13612823

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Registered trials

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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.