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Statements

Subject Item
n2:RIV%2F00209805%3A_____%2F14%3A%230000520%21RIV15-MSM-00209805
rdf:type
skos:Concept n19:Vysledek
rdfs:seeAlso
http://dx.doi.org/10.1016/j.aca.2014.04.056
dcterms:description
Recently, it was shown that electrochemical methods can be used for analysis of poorly water-soluble proteins and for study of their structural changes and intermolecular (protein-ligand) interactions. In this study, we focused on complex electrochemical investigation of recombinant protein FTT1103, a disulfide oxidoreductase with structural similarity to well described DsbA proteins. This thioredoxin-like periplasmic lipoprotein plays an important role in virulence of bacteria Francisella tularensis. For electrochemical analyses, adsorptive transfer (ex situ) square-wave voltammetry with pyrolytic graphite electrode, and alternating-current voltammetry and constant-current chronopotentiometric stripping analysis with mercury electrodes, including silver solid amalgam electrode (AgSAE) were used. AgSAE was used in poorly water-soluble protein analysis for the first time. In addition to basic redox, electrocatalytic and adsorption/desorption characterization of FTT1103, electrochemical methods were also used for sensitive determination of the protein at nanomolar level and study of its interaction with surface of AgSA microparticles. Proposed electrochemical protocol and AgSA surface-inhibition approach presented here could be used in future for biochemical studies focused on proteins associated with membranes as well as on those with disulfide oxidoreductase activity. Recently, it was shown that electrochemical methods can be used for analysis of poorly water-soluble proteins and for study of their structural changes and intermolecular (protein-ligand) interactions. In this study, we focused on complex electrochemical investigation of recombinant protein FTT1103, a disulfide oxidoreductase with structural similarity to well described DsbA proteins. This thioredoxin-like periplasmic lipoprotein plays an important role in virulence of bacteria Francisella tularensis. For electrochemical analyses, adsorptive transfer (ex situ) square-wave voltammetry with pyrolytic graphite electrode, and alternating-current voltammetry and constant-current chronopotentiometric stripping analysis with mercury electrodes, including silver solid amalgam electrode (AgSAE) were used. AgSAE was used in poorly water-soluble protein analysis for the first time. In addition to basic redox, electrocatalytic and adsorption/desorption characterization of FTT1103, electrochemical methods were also used for sensitive determination of the protein at nanomolar level and study of its interaction with surface of AgSA microparticles. Proposed electrochemical protocol and AgSA surface-inhibition approach presented here could be used in future for biochemical studies focused on proteins associated with membranes as well as on those with disulfide oxidoreductase activity.
dcterms:title
Investigation of protein FTT1103 electroactivity using carbon and mercury electrodes. Surface-inhibition approach for disulfide oxidoreductases using silver amalgam powder Investigation of protein FTT1103 electroactivity using carbon and mercury electrodes. Surface-inhibition approach for disulfide oxidoreductases using silver amalgam powder
skos:prefLabel
Investigation of protein FTT1103 electroactivity using carbon and mercury electrodes. Surface-inhibition approach for disulfide oxidoreductases using silver amalgam powder Investigation of protein FTT1103 electroactivity using carbon and mercury electrodes. Surface-inhibition approach for disulfide oxidoreductases using silver amalgam powder
skos:notation
RIV/00209805:_____/14:#0000520!RIV15-MSM-00209805
n3:aktivita
n4:P n4:I
n3:aktivity
I, P(ED2.1.00/03.0101), P(GA14-08032S)
n3:cisloPeriodika
Jun 9
n3:dodaniDat
n5:2015
n3:domaciTvurceVysledku
Bartošík, Martin n13:3521869 n13:3764915
n3:druhVysledku
n8:J
n3:duvernostUdaju
n16:S
n3:entitaPredkladatele
n11:predkladatel
n3:idSjednocenehoVysledku
22754
n3:idVysledku
RIV/00209805:_____/14:#0000520
n3:jazykVysledku
n7:eng
n3:klicovaSlova
disulfide bond forming protein; oxidoreductase; surface inhibition; membrane proteins
n3:klicoveSlovo
n9:membrane%20proteins n9:disulfide%20bond%20forming%20protein n9:surface%20inhibition n9:oxidoreductase
n3:kodStatuVydavatele
NL - Nizozemsko
n3:kontrolniKodProRIV
[74D08AA900F0]
n3:nazevZdroje
Analytica chimica acta
n3:obor
n15:CG
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
7
n3:projekt
n10:GA14-08032S n10:ED2.1.00%2F03.0101
n3:rokUplatneniVysledku
n5:2014
n3:svazekPeriodika
830
n3:tvurceVysledku
Dobeš, Petr Hernychová, Lenka Bartošík, Martin
n3:wos
000336390700003
s:issn
0003-2670
s:numberOfPages
9
n18:doi
10.1016/j.aca.2014.04.056