Evidence map›Paper›PMID 24052412›Full record

ArticleJournal of biomolecular NMR2013

HN(CA)N and HN(COCA)N experiments for assignment of large disordered proteins.

Xiao Liu, Daiwen Yang

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. HACANCOi: a new HJournal of biomolecular NMR · 2020
    Article
  2. Article
  3. Article
  4. Article
  5. Article
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

2 authors.

Xiao LiuDepartment of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore.
Daiwen Yang

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two new 3D HN-based experiments are proposed for backbone assignment of large disordered proteins. The spectra obtained with the new pulse schemes are free of redundant diagonal peaks (HiNi-Ni) and provide sequential correlations (HiNi-Ni+1 and HiNi-Ni-1) not only between adjacent non-proline residues but also between non-proline and proline residues. The experiments have been demonstrated on an intrinsically disordered protein with 306 amino acids including 64 proline residues. Using the two experiments, we obtained nearly complete assignments of backbone amides and proline (15)N spins except for 4 proline and 4 non-proline residues.

Indexed as

Nuclear Magnetic Resonance, BiomolecularAmino Acid MotifsAmino Acid SequenceIntrinsically Disordered ProteinsIntrinsically Disordered Proteins

Identifiers

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.