Evidence map›Paper›PMID 22946877›Full record

ArticleJournal of the American Chemical Society2012

Symmetry-constrained analysis of pulsed double electron-electron resonance (DEER) spectroscopy reveals the dynamic nature of the KcsA activation gate.

Olivier Dalmas, H Clark Hyde, Raymond E Hulse, Eduardo Perozo

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. ACS chemical biology · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. A Bayesian approach to quantifying uncertainty from experimental noise in DEER spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2016
    Article
  18. Article
  19. Article
  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

4 authors.

Olivier DalmasDepartment of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
H Clark Hyde
Raymond E Hulse
Eduardo Perozo

Funding

Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI NAKAMOTO, ROBERT K. · 2010 to 2017
$31.9M
The Electrophysiological Studies of Voltage Gated ChannelsR01GM030376 · NIGMS · UNIVERSITY OF CHICAGO · PI BEZANILLA, FRANCISCO J · 1985 to 2025
$9.1M
HIGH RESOLUTION STRUCTURAL DYNAMICS OF K CHANNELSR01GM057846 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PEROZO, EDUARDO A · 1998 to 2018
$7.4M
ELECTROPHYSIOLOGICAL STUDIES OF VOLTAGE GATED CHANNELSR37GM030376 · NIGMS · UNIVERSITY OF CHICAGO · PI BEZANILLA, FRANCISCO J · 1999 to 2008
$3.7M
Structural basis for transmembrane Mg2+ transportR01GM088406 · NIGMS · UNIVERSITY OF CHICAGO · PI PEROZO, EDUARDO A · 2009 to 2012
$1.3M
NIGMS NIH HHS GM030376NIGMS NIH HHS GM088406NIGMS NIH HHS R01 GM057846NIGMS NIH HHS R01 GM088406NIGMS NIH HHS U54 GM087519
6 · The paper itself

Abstract

Distance determination from an echo intensity modulation obtained by pulsed double electron-electron resonance (DEER) experiment is a mathematically ill-posed problem. Tikhonov regularization yields distance distributions that can be difficult to interpret, especially in a system with multiple discrete distance distributions. Here, we show that by using geometric fit constraints in symmetric homo-oligomeric protein systems, we were able to increase the accuracy of a model-based fit solution based on a sum of Rice distributions. Our approach was validated on two different ion channels of known oligomeric states, KcsA (tetramer) and CorA (pentamer). Statistical analysis of the resulting fits was integrated within our method to help the experimenter evaluate the significance of a symmetry-constrained vs standard model distribution fit and to examine multidistance confidence regions. This approach was used to quantitatively evaluate the role of the C-terminal domain (CTD) on the flexibility and conformation of the activation gate of the K(+) channel KcsA. Our analysis reveals a significant increase in the dynamics of the inner bundle gate upon opening. Also, it explicitly demonstrates the degree to which the CTD restricts the motion of the lower gate at rest and during activation gating.

Indexed as

Ion Channel GatingBacterial ProteinsElectron Spin Resonance SpectroscopyModels, MolecularPotassium ChannelsProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiaryReproducibility of ResultsStreptomyces lividansBacterial ProteinsPotassium Channelsprokaryotic potassium channel

Identifiers

PMID22946877
PMCPMC3845908

What OpenQuestion holds

Textmetadata
LicenceTDM
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.