Evidence map›Paper›PMID 26477252›Full record

ArticleMethods in enzymology2015

Ionizable Nitroxides for Studying Local Electrostatic Properties of Lipid Bilayers and Protein Systems by EPR.

Maxim A Voinov, Alex I Smirnov

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.0field-weighted citation impact, top 6% 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

4 citing papers in PubMed, 13 citations in OpenAlex.

  1. Real-Time Monitoring of Photoinduced pH Jumps byThe journal of physical chemistry letters · 2024
    Article
  2. Article
  3. Direct Prediction of EPR Spectra from Lipid Bilayers: Understanding Structure and Dynamics in Biological Membranes.Chemphyschem : a European journal of chemical physics and physical chemistry · 2018
    Article
  4. 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

2 authors at 1 institution in 1 country.

Maxim A VoinovDepartment of Chemistry, North Carolina State University, Raleigh, North Carolina, USA.
Alex I SmirnovDepartment of Chemistry, North Carolina State University, Raleigh, North Carolina, USA. Electronic address: aismirno@ncsu.edu.
North Carolina State University · US

Funding

Time-domain/ELDOR EPR SpectrometerS10RR023614 · NCRR · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI SMIRNOV, ALEX I. · 2009 to 2009
$500k
NCRR NIH HHS RR023614NCRR NIH HHS S10 RR023614
6 · The paper itself

Abstract

Electrostatic interactions are known to play a major role in the myriad of biochemical and biophysical processes. Here, we describe biophysical methods to probe local electrostatic potentials of proteins and lipid bilayer systems that are based on an observation of reversible protonation of nitroxides by electron paramagnetic resonance (EPR). Two types of probes are described: (1) methanethiosulfonate derivatives of protonatable nitroxides for highly specific covalent modification of the cysteine's sulfhydryl groups and (2) spin-labeled phospholipids with a protonatable nitroxide tethered to the polar head group. The probes of both types report on their ionization state through changes in magnetic parameters and degree of rotational averaging, thus, allowing the electrostatic contribution to the interfacial pKa of the nitroxide, and, therefore, the local electrostatic potential to be determined. Due to their small molecular volume, these probes cause a minimal perturbation to the protein or lipid system. Covalent attachment secures the position of the reporter nitroxides. Experimental procedures to characterize and calibrate these probes by EPR, and also the methods to analyze the EPR spectra by simulations are outlined. The ionizable nitroxide labels and the nitroxide-labeled phospholipids described so far cover an exceptionally wide range of ca. 2.5-7.0 pH units, making them suitable to study a broad range of biophysical phenomena, especially at the negatively charged lipid bilayer surfaces. The rationale for selecting proper electrostatically neutral interface for probe calibration, and examples of lipid bilayer surface potential studies, are also described.

Indexed as

Spin LabelsAnimalsElectron Spin Resonance SpectroscopyHumansHydrogen-Ion ConcentrationLipid BilayersNitrogen OxidesProteinsProtonsStatic ElectricitySulfhydryl CompoundsLipid BilayersNitrogen OxidesnitroxylProteinsProtonsSpin LabelsSulfhydryl CompoundsElectrostatic potentialEPRGouy–Chapman theoryImidazolidineImidazolineIonizable nitroxidesLipid bilayerpH-sensitive nitroxidesSite-directed spin labelingSurface chargeSurface potential

Identifiers

PMID26477252
PMCPMC5008871
OpenAlexW1843330539

What OpenQuestion holds

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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.