Evidence map›Paper›PMID 34272395›Full record

ArticleNature communications2021

Correlation of membrane protein conformational and functional dynamics.

Raghavendar Reddy Sanganna Gari, Joel José Montalvo-Acosta, George R Heath, Yining Jiang, Xiaolong Gao, Crina M Nimigean, Christophe Chipot, Simon Scheuring

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Review
  3. HS-AFM Applications to Study Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
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  9. Review
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  14. Probing both sides of the story.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. 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

8 authors at 3 institutions in 3 countries.

Raghavendar Reddy Sanganna GariWeill Cornell Medicine, Department of Anesthesiology, New York, NY, USA.
Joel José Montalvo-AcostaLaboratoire International Associé CNRS and University of Illinois at Urbana-Champaign, Université de Lorraine, Vandœuvre-lès-Nancy, France.
George R HeathWeill Cornell Medicine, Department of Anesthesiology, New York, NY, USA.ORCID 0000-0001-6431-2191
Yining JiangWeill Cornell Medicine, Department of Physiology and Biophysics, New York, NY, USA.
Xiaolong GaoWeill Cornell Medicine, Department of Anesthesiology, New York, NY, USA.ORCID 0000-0001-8933-9286
Crina M NimigeanWeill Cornell Medicine, Department of Anesthesiology, New York, NY, USA.ORCID 0000-0002-6254-4447
Christophe ChipotLaboratoire International Associé CNRS and University of Illinois at Urbana-Champaign, Université de Lorraine, Vandœuvre-lès-Nancy, France. chipot@illinois.edu.ORCID 0000-0002-9122-1698
Simon ScheuringWeill Cornell Medicine, Department of Anesthesiology, New York, NY, USA. sis2019@med.cornell.edu.ORCID 0000-0003-3534-069X
Cornell University · USCentre National de la Recherche Scientifique · FRUniversity of Leeds · GB

Funding

Structural dynamics in cyclic nucleotide-modulated channelsR01GM124451 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI NIMIGEAN, CRINA M · 2017 to 2024
$3.2M
High-speed atomic force microscopy with microsecond time resolution for the study of channels and transportersR01NS110790 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI Simon Scheuring · 2019 to 2026
$2.4M
NIGMS NIH HHS R01 GM124451NINDS NIH HHS R01 NS110790
6 · The paper itself

Abstract

Conformational changes in ion channels lead to gating of an ion-conductive pore. Ion flux has been measured with high temporal resolution by single-channel electrophysiology for decades. However, correlation between functional and conformational dynamics remained difficult, lacking experimental techniques to monitor sub-millisecond conformational changes. Here, we use the outer membrane protein G (OmpG) as a model system where loop-6 opens and closes the β-barrel pore like a lid in a pH-dependent manner. Functionally, single-channel electrophysiology shows that while closed states are favored at acidic pH and open states are favored at physiological pH, both states coexist and rapidly interchange in all conditions. Using HS-AFM height spectroscopy (HS-AFM-HS), we monitor sub-millisecond loop-6 conformational dynamics, and compare them to the functional dynamics from single-channel recordings, while MD simulations provide atomistic details and energy landscapes of the pH-dependent loop-6 fluctuations. HS-AFM-HS offers new opportunities to analyze conformational dynamics at timescales of domain and loop fluctuations.

Indexed as

Bacterial Outer Membrane ProteinsElectrophysiologyEscherichia coliEscherichia coli ProteinsHydrogen-Ion ConcentrationIon Channel GatingIon ChannelsLipid BilayersMicroscopy, Atomic ForceMolecular Dynamics SimulationPorinsProtein ConformationProtein Conformation, beta-StrandRecombinant ProteinsSpectrum AnalysisStructure-Activity RelationshipBacterial Outer Membrane ProteinsEscherichia coli ProteinsIon ChannelsLipid BilayersOmpG protein, E coliPorinsRecombinant Proteins

Identifiers

PMID34272395
PMCPMC8285522
OpenAlexW3179942155

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.