Evidence map›Paper›PMID 19940918›Full record

ArticleNature2009

Structure and hydration of membranes embedded with voltage-sensing domains.

Dmitriy Krepkiy, Mihaela Mihailescu, J Alfredo Freites, Eric V Schow, David L Worcester, Klaus Gawrisch, Douglas J Tobias, Stephen H White, Kenton J Swartz

Abstract read
In one paragraph

Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing 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

105 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Special issue for Klaus Gawrisch.Biophysical journal · 2023
    Article
  9. Tracking Membrane Protein Dynamics in Real Time.The Journal of membrane biology · 2021
    Review
  10. Article
  11. Comparison of KHandbook of experimental pharmacology · 2021
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Essay on Biomembrane Structure.The Journal of membrane biology · 2019
    Review
  18. Review
  19. Article
  20. Review

45 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Dmitriy KrepkiyMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, USA.
Mihaela Mihailescu
J Alfredo Freites
Eric V Schow
David L Worcester
Klaus Gawrisch
Douglas J Tobias
Stephen H White
Kenton J Swartz

Funding

Gating mechanisms and pharmacology of voltage-activated ion channelsZIANS002945 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI SWARTZ, KENTON · 2009 to 2025
$44.2M
NMR Investigations Of Cell Membrane StructureZIAAA000003 · NIAAA · NATIONAL INSTITUTE ON ALCOHOL ABUSE AND ALCOHOLISM · PI GAWRISCH, KLAUS · 2009 to 2020
$23.2M
Project 3: Structural Studies of Voltage-Gated Potassium Channels as FunctionP01GM086685 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WORCESTER, DAVID · 2009 to 2013
$6.7M
Cold Neutrons For Biology And TechnologyR01RR014812 · NCRR · UNIVERSITY OF CALIFORNIA IRVINE · PI WHITE, STEPHEN H. · 2001 to 2005
$5.4M
Molecular Genetics of Drosophila Hybrid LethalityR01GM074737 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BARBASH, DANIEL A · 2005 to 2022
$4.7M
Membrane Protein Folding and AssemblyR01GM074637 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2006 to 2020
$4.5M
Intramural NIH HHS ZIA NS002945NCRR NIH HHS R01 RR014812NIGMS NIH HHS GM74737NIGMS NIH HHS GM86685NIGMS NIH HHS P01 GM086685NIGMS NIH HHS R01 GM074637NIGMS NIH HHS R01 GM074737
6 · The paper itself

Abstract

Despite the growing number of atomic-resolution membrane protein structures, direct structural information about proteins in their native membrane environment is scarce. This problem is particularly relevant in the case of the highly charged S1-S4 voltage-sensing domains responsible for nerve impulses, where interactions with the lipid bilayer are critical for the function of voltage-activated ion channels. Here we use neutron diffraction, solid-state nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics simulations to investigate the structure and hydration of bilayer membranes containing S1-S4 voltage-sensing domains. Our results show that voltage sensors adopt transmembrane orientations and cause a modest reshaping of the surrounding lipid bilayer, and that water molecules intimately interact with the protein within the membrane. These structural findings indicate that voltage sensors have evolved to interact with the lipid membrane while keeping energetic and structural perturbations to a minimum, and that water penetrates the membrane, to hydrate charged residues and shape the transmembrane electric field.

Indexed as

Membrane PotentialsArchaeal ProteinsCircular DichroismLipid BilayersMembrane LipidsModels, MolecularMolecular Dynamics SimulationNeutron DiffractionNuclear Magnetic Resonance, BiomolecularPotassium Channels, Voltage-GatedProtein Structure, TertiarySpectrometry, FluorescenceWaterArchaeal ProteinsLipid BilayersMembrane LipidsPotassium Channels, Voltage-GatedWater

Identifiers

PMID19940918
PMCPMC2784928

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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.