Evidence map›Paper›PMID 18850278›Full record

ArticleJournal of biomolecular NMR2008

Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP.

Kristofer Modig, Flemming M Poulsen

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Article in Journal of biomolecular NMR, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. What DrivesBiophysical journal · 2018
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cooperative formation of native-like tertiary contacts in the ensemble of unfolded states of a four-helix protein.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  11. 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.

Kristofer ModigStructural Biology and NMR Laboratory, Department of Molecular Biology, University of Copenhagen, Copenhagen Biocenter, Ole Maaløes Vej 5, 2200, Copenhagen, Denmark. kristofer.modig@bpc.lu.se
Flemming M Poulsen

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have investigated the acid-unfolded state of acyl-coenzyme A binding protein (ACBP) using 15N laboratory frame nuclear magnetic resonance (NMR) relaxation experiments at three magnetic field strengths. The data have been analyzed using standard model-free fitting and models involving distribution of correlation times. In particular, a model-independent method of analysis that does not assume any analytical form for the correlation time distribution is proposed. This method explains correlations between model-free parameters and the analytical distribution parameters found by other authors. The analysis also shows that the relaxation data are consistent with and complementary to information obtained from other parameters, especially secondary chemical shifts and residual dipolar couplings, and strengthens the conclusions of previous observations that three out of the four regions that form helices in the native structure appear to contain residual secondary structure also in the acid-denatured state.

Indexed as

Protein DenaturationAcidsDiazepam Binding InhibitorNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryAcidsDiazepam Binding Inhibitor

Identifiers

What OpenQuestion holds

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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.