Evidence map›Paper›PMID 27860003›Full record

ArticleAngewandte Chemie (International ed. in English)2016

Long Distance Measurements up to 160 Å in the GroEL Tetradecamer Using Q-Band DEER EPR Spectroscopy.

Thomas Schmidt, Marielle A Wälti, James L Baber, Eric J Hustedt, G Marius Clore

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing 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

83 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. The soluble state of the HIV-1 Vpu protein forms a complex with CaProtein science : a publication of the Protein Society · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Investigating the Conformational Diversity of the TMR-3 Aptamer.Journal of the American Chemical Society · 2025
    Article
  14. Protein Modeling with DEER Spectroscopy.Annual review of biophysics · 2025
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Endogenous Cu(II) Labeling for Distance Measurements on Proteins by EPR.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  20. Expanded Functionality and Portability for the Colvars Library.The journal of physical chemistry. B · 2024
    Article

23 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

5 authors.

Thomas SchmidtLaboratory of Chemical Physics, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892-0520, USA.
Marielle A WältiLaboratory of Chemical Physics, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892-0520, USA.
James L BaberLaboratory of Chemical Physics, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892-0520, USA.
Eric J HustedtDepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN, 37232, USA.
G Marius CloreLaboratory of Chemical Physics, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892-0520, USA.ORCID 0000-0003-3809-1027

Funding

Structure and Dynamics Of Macromolecules In Solution By NMRZIADK029023 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CLORE, GIDEON · 2009 to 2025
$41.5M
NMR STUDIES OF THREE-DIMENSIONAL STRUCTURE OF MACROMOLECULES IN SOLUTIONZ01DK029023 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CLORE, G. MARIUS · 1988 to 2008
$949k
Intramural NIH HHS Z01 DK029023
6 · The paper itself

Abstract

Current distance measurements between spin-labels on multimeric protonated proteins using double electron-electron resonance (DEER) EPR spectroscopy are generally limited to the 15-60 Å range. Here we show how DEER experiments can be extended to dipolar evolution times of ca. 80 μs, permitting distances up to 170 Å to be accessed in multimeric proteins. The method relies on sparse spin-labeling, supplemented by deuteration of protein and solvent, to minimize the deleterious impact of multispin effects and substantially increase the apparent spin-label phase memory relaxation time, complemented by high sensitivity afforded by measurements at Q-band. We demonstrate the approach using the tetradecameric molecular machine GroEL as an example. Two engineered surface-exposed mutants, R268C and E315C, are used to measure pairwise distance distributions with mean values ranging from 20 to 100 Å and from 30 to 160 Å, respectively, both within and between the two heptameric rings of GroEL. The measured distance distributions are consistent with the known crystal structure of apo GroEL. The methodology presented here should significantly expand the use of DEER for the structural characterization of conformational changes in higher order oligomers.

Indexed as

Protein MultimerizationChaperonin 60Electron Spin Resonance SpectroscopyEscherichia coli K12Escherichia coli ProteinsModels, MolecularPoint MutationChaperonin 60Escherichia coli Proteinsbiophysicschemical physicsEPR spectroscopyspectroscopic methodsstructural biology

Identifiers

PMID27860003
PMCPMC5166617

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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.