Evidence map›Paper›PMID 26419214›Full record

ArticleChemphyschem : a European journal of chemical physics and physical chemistry2015

How Sensitive is the Amide I Vibration of the Polypeptide Backbone to Electric Fields?

Kwang-Im Oh, Giacomo Fiorin, Feng Gai

Abstract read
In one paragraph

Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

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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

11 citing papers in PubMed.

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  8. Perspective: THz-driven nuclear dynamics from solids to molecules.Structural dynamics (Melville, N.Y.) · 2017
    Article
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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

3 authors.

Kwang-Im OhDepartment of Chemistry, University of Pennsylvania, 231 S. 34th Street, Philadelphia, PA, 19104-6323, USA.
Giacomo FiorinInstitute for Computational Molecular Science, Temple University, 1925 North 12th Street, Philadelphia, PA, 19122-1801, USA.
Feng GaiDepartment of Chemistry, University of Pennsylvania, 231 S. 34th Street, Philadelphia, PA, 19104-6323, USA. gai@sas.upenn.edu.

Funding

ULTRAFAST OPTICAL PROCESSES LABORATORYP41GM104605 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2012 to 2017
$5.6M
NIGMS NIH HHS P41 GM104605
6 · The paper itself

Abstract

Site-selective isotopic labeling of amide carbonyls offers a nonperturbative means to introduce a localized infrared probe into proteins. Although this strategy has been widely used to investigate various biological questions, the dependence of the underlying amide I vibrational frequency on electric fields (or Stark tuning rate) has not been fully determined, which prevents it from being used in a quantitative manner in certain applications. Herein, through the use of experiments and molecular dynamics simulations, the Stark tuning rate of the amide I vibration of an isotopically labeled backbone carbonyl in a transmembrane α-helix is determined to be approximately 1.4 cm(-1) /(MV/cm). This result provides a quantitative basis for using this vibrational model to assess local electric fields in proteins, among other applications. For instance, by using this value, we are able to show that the backbone region of a dipeptide has a surprisingly low dielectric constant.

Indexed as

ElectricityMolecular Dynamics SimulationVibrationAmidesPeptidesAmidesPeptidesamide I vibrationIR spectroscopymembrane electric fieldmolecular dynamicsStark tuning rate

Identifiers

PMID26419214
PMCPMC4715676

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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.