Evidence map›Paper›PMID 21184138›Full record

ArticleJournal of biomolecular NMR2011

Residual dipolar couplings: are multiple independent alignments always possible?

Victoria A Higman, Jonathan Boyd, Lorna J Smith, Christina Redfield

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. On the complementarity of X-ray and NMR data.Journal of structural biology: X · 2020
    Article
  6. Article
  7. Solution structure of sperm lysin yields novel insights into molecular dynamics of rapid protein evolution.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. 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

4 authors.

Victoria A HigmanDepartment of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, UK.
Jonathan Boyd
Lorna J Smith
Christina Redfield

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 079440
6 · The paper itself

Abstract

RDCs for the 14 kDa protein hen egg-white lysozyme (HEWL) have been measured in eight different alignment media. The elongated shape and strongly positively charged surface of HEWL appear to limit the protein to four main alignment orientations. Furthermore, low levels of alignment and the protein's interaction with some alignment media increases the experimental error. Together with heterogeneity across the alignment media arising from constraints on temperature, pH and ionic strength for some alignment media, these data are suitable for structure refinement, but not the extraction of dynamic parameters. For an analysis of protein dynamics the data must be obtained with very low errors in at least three or five independent alignment media (depending on the method used) and so far, such data have only been reported for three small 6-8 kDa proteins with identical folds: ubiquitin, GB1 and GB3. Our results suggest that HEWL is likely to be representative of many other medium to large sized proteins commonly studied by solution NMR. Comparisons with over 60 high-resolution crystal structures of HEWL reveal that the highest resolution structures are not necessarily always the best models for the protein structure in solution.

Indexed as

Models, MolecularNuclear Magnetic Resonance, BiomolecularMuramidaseProtein ConformationSolutionsUbiquitinhen egg lysozymeMuramidaseSolutionsUbiquitin

Identifiers

PMID21184138
PMCPMC3020303

What OpenQuestion holds

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LicenceCC BY-NC
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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.