Evidence map›Paper›PMID 28699064›Full record

ArticleJournal of the American Society for Mass Spectrometry2017

Joule Heating and Thermal Denaturation of Proteins in Nano-ESI Theta Tips.

Feifei Zhao, Sarah M Matt, Jiexun Bu, Owen G Rehrauer, Dor Ben-Amotz, Scott A McLuckey

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

9 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Electrospray Photochemical Oxidation of Proteins.Journal of the American Society for Mass Spectrometry · 2019
    Article
  8. Article
  9. On the intersection of electrochemistry and mass spectrometry.Current opinion in electrochemistry · 2019
    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

6 authors at 1 institution in 1 country.

Feifei ZhaoDepartment of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN, 47907-2084, USA.
Sarah M MattDepartment of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN, 47907-2084, USA.
Jiexun BuDepartment of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN, 47907-2084, USA.
Owen G RehrauerDepartment of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN, 47907-2084, USA.
Dor Ben-AmotzDepartment of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN, 47907-2084, USA.
Scott A McLuckeyDepartment of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN, 47907-2084, USA. mcluckey@purdue.edu.ORCID 0000-0002-1648-5570
Purdue University West Lafayette · US

Funding

Gas-phase Bio-conjugation in the Tandem Mass Spectrometry of Peptides, Proteins,R37GM045372 · NIGMS · PURDUE UNIVERSITY · PI MCLUCKEY, SCOTT A · 2014 to 2023
$3.1M
NIGMS NIH HHS R37-045372NIGMS NIH HHS R37 GM045372
6 · The paper itself

Abstract

Electro-osmotically induced Joule heating in theta tips and its effect on protein denaturation were investigated. Myoglobin, equine cytochrome c, bovine cytochrome c, and carbonic anhydrase II solutions were subjected to electro-osmosis in a theta tip and all of the proteins were denatured during the process. The extent of protein denaturation was found to increase with the applied square wave voltage and electrolyte concentration. The solution temperature at the end of a theta tip was measured directly by Raman spectroscopy and shown to increase with the square wave voltage, thereby demonstrating the effect of Joule heating through an independent method. The electro-osmosis of a solution comprised of myoglobin, bovine cytochrome c, and ubiquitin demonstrated that the magnitude of Joule heating that causes protein denaturation is positively correlated with protein melting temperature. This allows for a quick determination of a protein's relative thermal stability. This work establishes a fast, novel method for protein conformation manipulation prior to MS analysis and provides a temperature-controllable platform for the study of processes that take place in solution with direct coupling to mass spectrometry. Graphical Abstract ᅟ.

Indexed as

Protein DenaturationAcetatesAnimalsCattleCytochromes cHorsesHot TemperatureMyoglobinProteinsSpectrometry, Mass, Electrospray IonizationSpectrum Analysis, RamanTransition TemperatureUbiquitinAcetatesammonium acetateCytochromes cMyoglobinProteinsUbiquitinElectro-osmosisJoule heatingProtein denaturationTheta tip

Identifiers

PMID28699064
PMCPMC5693742
OpenAlexW2734677184

What OpenQuestion holds

Textmetadata
LicenceTDM
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.