Evidence map›Paper›PMID 33576633›Full record

ArticleThe journal of physical chemistry letters2021

Structure Changes of a Membrane Polypeptide under an Applied Voltage Observed with Surface-Enhanced 2D IR Spectroscopy.

Erin R Birdsall, Megan K Petti, Vivek Saraswat, Joshua S Ostrander, Michael S Arnold, Martin T Zanni

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Erin R BirdsallDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID http://orcid.org/0000-0002-1972-7475
Megan K PettiDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID http://orcid.org/0000-0001-7381-9701
Vivek SaraswatDepartment of Materials Science and Engineering, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID http://orcid.org/0000-0001-5095-3078
Joshua S OstranderDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID http://orcid.org/0000-0002-6338-6639
Michael S ArnoldDepartment of Materials Science and Engineering, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.
Martin T ZanniDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID http://orcid.org/0000-0001-7191-9768
University of Wisconsin–Madison · US

Funding

BIOTECHNOLOGY TRAINING PROGRAMT32GM008349 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI FOX, BRIAN G · 1989 to 2019
$22.5M
A new perspesective on ion conductance and structural dynamics of ion channels using 2D IRR01GM135936 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ZANNI, MARTIN T · 2020 to 2025
$1.7M
Examining Amyloid-β Structure During the Progression of Alzheimer’s Disease using an Immuno-2DIR-SensorR21AG061602 · NIA · UNIVERSITY OF WISCONSIN-MADISON · PI ZANNI, MARTIN T · 2019 to 2020
$409k
NIA NIH HHS R21 AG061602NIGMS NIH HHS R01 GM135936NIGMS NIH HHS T32 GM008349
6 · The paper itself

Abstract

The structures of many membrane-bound proteins and polypeptides depend on the membrane potential. However, spectroscopically studying their structures under an applied field is challenging, because a potential is difficult to generate across more than a few bilayers. We study the voltage-dependent structures of the membrane-bound polypeptide, alamethicin, using a spectroelectrochemical cell coated with a rough, gold film to create surface plasmons. The plasmons sufficiently enhance the 2D IR signal to measure a single bilayer. The film is also thick enough to conduct current and thereby apply a potential. The 2D IR spectra resolve features from both 3

Indexed as

AlamethicinAmino Acid SequenceBiomedical EnhancementLipid BilayersMembrane PotentialsMembrane ProteinsMolecular Dynamics SimulationProtein ConformationSpectrophotometry, InfraredSurface PropertiesVibrationAlamethicinLipid BilayersMembrane Proteins

Identifiers

PMID33576633
PMCPMC8162810
OpenAlexW3128463426

What OpenQuestion holds

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LicenceTDM
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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.