Evidence map›Paper›PMID 20041279›Full record

ArticleJournal of biomolecular NMR2010

Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts.

Yang Shen, Ad Bax

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing 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

75 citing papers in PubMed.

  1. Article
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  5. Conformational dynamics in specialized CProtein science : a publication of the Protein Society · 2025
    Article
  6. Article
  7. The conformational landscape of fold-switcher KaiB is tuned to the circadian rhythm timescale.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
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  13. Article
  14. Intrinsic disorder and conformational coexistence in auxin coreceptors.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

15 more citing papers are in PubMed but not listed here.

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.

Yang ShenLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Building 5, Room 126, Bethesda, MD, 20892-0520, USA. bax@nih.gov
Ad Bax

Funding

Methods to accelerate protein structure determination by solution NMRZIADK029046 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BAX, ADRIAAN · 2009 to 2025
$12.8M
Intramural NIH HHS ZIA DK029046
6 · The paper itself

Abstract

We present a program, named Promega, to predict the Xaa-Pro peptide bond conformation on the basis of backbone chemical shifts and the amino acid sequence. Using a chemical shift database of proteins of known structure together with the PDB-extracted amino acid preference of cis Xaa-Pro peptide bonds, a cis/trans probability score is calculated from the backbone and (13)C(beta) chemical shifts of the proline and its neighboring residues. For an arbitrary number of input chemical shifts, which may include Pro-(13)C(gamma), Promega calculates the statistical probability that a Xaa-Pro peptide bond is cis. Besides its potential as a validation tool, Promega is particularly useful for studies of larger proteins where Pro-(13)C(gamma) assignments can be challenging, and for on-going efforts to determine protein structures exclusively on the basis of backbone and (13)C(beta) chemical shifts.

Indexed as

Nuclear Magnetic Resonance, BiomolecularPeptidesProlinePeptidesProline

Identifiers

PMID20041279
PMCPMC2847849

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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.