Evidence map›Paper›PMID 26286372›Full record

ArticleScientific reports2015

Long- and Short-Range Electrostatic Fields in GFP Mutants: Implications for Spectral Tuning.

M Drobizhev, P R Callis, R Nifosì, G Wicks, C Stoltzfus, L Barnett, T E Hughes, P Sullivan, A Rebane

Abstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

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  13. Mechanism and bottlenecks in strand photodissociation of split green fluorescent proteins (GFPs).Proceedings of the National Academy of Sciences of the United States of America · 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

9 authors.

M DrobizhevDepartment of Physics, Montana State University, Bozeman MT 59717.
P R CallisDepartment of Chemistry and Biochemistry, Montana State University, Bozeman MT 59717.
R NifosìNEST, Istituto Nanoscienze-CNR and Scuola Normale Superiore, I-56127 Pisa, Italy.
G WicksDepartment of Physics, Montana State University, Bozeman MT 59717.
C StoltzfusDepartment of Physics, Montana State University, Bozeman MT 59717.
L BarnettDepartment of Cell Biology and Neuroscience, Montana State University, Bozeman MT 59717.
T E HughesDepartment of Cell Biology and Neuroscience, Montana State University, Bozeman MT 59717.
P SullivanDepartment of Chemistry and Biochemistry, Montana State University, Bozeman MT 59717.
A Rebane1] Department of Physics, Montana State University, Bozeman MT 59717 [2] National Insitute of Chemical Physics and Biophysics, Tallinn 12618, Estonia.

Funding

Genetically-Encoded Voltage Probe DevelopmentR01NS083875 · NINDS · JOHN B. PIERCE LABORATORY, INC. · PI HUGHES, THOMAS E, NITABACH, MICHAEL · 2013 to 2016
$2.3M
All-optical molecular voltmeter for measuring electric fields in proteinsR01GM098083 · NIGMS · MONTANA STATE UNIVERSITY - BOZEMAN · PI REBANE, ALEKSANDER · 2011 to 2014
$961k
NIGMS NIH HHS R01 GM 098083NIGMS NIH HHS R01 GM098083NINDS NIH HHS 1 R01 NS083875-01NINDS NIH HHS R01 NS083875
6 · The paper itself

Abstract

The majority of protein functions are governed by their internal local electrostatics. Quantitative information about these interactions can shed light on how proteins work and allow for improving/altering their performance. Green fluorescent protein (GFP) and its mutation variants provide unique optical windows for interrogation of internal electric fields, thanks to the intrinsic fluorophore group formed inside them. Here we use an all-optical method, based on the independent measurements of transition frequency and one- and two-photon absorption cross sections in a number of GFP mutants to evaluate these internal electric fields. Two physical models based on the quadratic Stark effect, either with or without taking into account structural (bond-length) changes of the chromophore in varying field, allow us to separately evaluate the long-range and the total effective (short- and long-range) fields. Both types of the field quantitatively agree with the results of independent molecular dynamic simulations, justifying our method of measurement.

Indexed as

MutationStatic ElectricityAnionsElectronsGreen Fluorescent ProteinsHydrogen BondingModels, TheoreticalMolecular Dynamics SimulationSolventsSpectrometry, FluorescenceSpectrum AnalysisWaterAnionsGreen Fluorescent ProteinsSolventsWater

Identifiers

PMID26286372
PMCPMC4541067

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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.