Evidence map›Paper›PMID 15189846›Full record

ArticleBiophysical journal2004

Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases.

Markus Zweckstetter, Gerhard Hummer, Ad Bax

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
4.6field-weighted citation impact, top 4% of its field
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

56 citing papers in PubMed, 117 citations in OpenAlex.

  1. Conformational ensembles explain NMR spectra of frozen intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2023
    Article
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  5. Paper-based fluorogenic RNA aptamer sensors for label-free detection of small molecules.Analytical methods : advancing methods and applications · 2020
    Article
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  8. Review
  9. Article
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  11. Review
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  14. NMR studies of dynamic biomolecular conformational ensembles.Progress in nuclear magnetic resonance spectroscopy · 2015
    Review
  15. Article
  16. Article
  17. Basic Tilted Helix Bundle - a new protein fold in human FKBP25/FKBP3 and HectD1.Biochemical and biophysical research communications · 2014
    Article
  18. Article
  19. Review
  20. 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

3 authors at 3 institutions in 2 countries.

Markus ZweckstetterMax Planck Institute for Biophysical Chemistry, Am Fassberg, Gottingen, Germany. mzwecks@gwdg.de
Gerhard Hummer
Ad Bax
Max Planck Institute for Biophysical Chemistry · DENational Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Theory and simulation of protein dynamics, folding, and functionZIADK029033 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HUMMER, GERHARD · 2009 to 2013
$3.3M
Theory &simulation of protein dynamics, folding,&functZ01DK029033 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HUMMER, GERHARD · 2000 to 2008
$960k
Study of membrane protein structure by NMR spectroscopy: the KcsA channelZ01DK029020 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BAX, AD - · 1986 to 2008
$427k
6 · The paper itself

Abstract

Alignment of macromolecules in nearly neutral aqueous lyotropic liquid-crystalline media such as bicelles, commonly used in macromolecular NMR studies, can be predicted accurately by a steric obstruction model (Zweckstetter and Bax, 2000). A simple extension of this model is described that results in improved predictions for both the alignment orientation and magnitude of protein and DNA solutes in charged nematic media, such as the widely used medium of filamentous phage Pf1. The extended model approximates the electrostatic interaction between a solute and an ordered phage particle as that between the solute's surface charges and the electric field of the phage. The model is evaluated for four different proteins and a DNA oligomer. Results indicate that alignment in charged nematic media is a function not only of the solute's shape, but also of its electric multipole moments of net charge, dipole, and quadrupole. The relative importance of these terms varies greatly from one macromolecule to another, and evaluation of the experimental data indicates that these terms scale differently with ionic strength. For several of the proteins, the calculated alignment is sensitive to the precise position of the charged groups on the protein surface. This suggests that NMR alignment measurements can potentially be used to probe protein electrostatics. Inclusion of electrostatic interactions in addition to steric effects makes the extended model applicable to all liquid crystals used in biological NMR to date.

Indexed as

Models, TheoreticalAlgorithmsBacterial ProteinsBacteriophage Pf1Escherichia coliEscherichia coli ProteinsNuclear Magnetic Resonance, BiomolecularSolutionsUbiquitinBacterial ProteinsDinI protein, E coliEscherichia coli ProteinsSolutionsUbiquitin

Identifiers

PMID15189846
PMCPMC1304251
OpenAlexW2150483412

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.