Protein structural transition at negatively charged electrode surfaces. Effects of temperature and current density

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F15%3A00447601" target="_blank" >RIV/68081707:_____/15:00447601 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.electacta.2015.06.009" target="_blank" >http://dx.doi.org/10.1016/j.electacta.2015.06.009</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.electacta.2015.06.009" target="_blank" >10.1016/j.electacta.2015.06.009</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Protein structural transition at negatively charged electrode surfaces. Effects of temperature and current density

Popis výsledku v původním jazyce

Earlier it was shown that surface-attached bovine serum albumin undergoes ionic strength-induced structural transition at mercury electrodes. Using constant current chronopotentiometric stripping (CPS) here we show that this electric field-driven transition is influenced also by other factors, such as temperature, current density, and particularly by the time of surface-attached protein exposure to the negative potentials. For example, 1 s exposure to -1.6 V (against Ag/AgC1/3 M KC1) results in the protein denaturation. Exposures longer than 1 s resulted in protein denaturation even at less negative potentials. On the other hand, in CPS much shorter exposure times can be used. Exposing the surface-attached protein to negative potentials for ms time intervals the protein stability can be tested at different current densities. We investigated several proteins such as bovine and human serum albumins, ovalbumin, ot-macroglobulin and ot-synuclein, which showed various profiles in dependence

Název v anglickém jazyce

Protein structural transition at negatively charged electrode surfaces. Effects of temperature and current density

Popis výsledku anglicky

Earlier it was shown that surface-attached bovine serum albumin undergoes ionic strength-induced structural transition at mercury electrodes. Using constant current chronopotentiometric stripping (CPS) here we show that this electric field-driven transition is influenced also by other factors, such as temperature, current density, and particularly by the time of surface-attached protein exposure to the negative potentials. For example, 1 s exposure to -1.6 V (against Ag/AgC1/3 M KC1) results in the protein denaturation. Exposures longer than 1 s resulted in protein denaturation even at less negative potentials. On the other hand, in CPS much shorter exposure times can be used. Exposing the surface-attached protein to negative potentials for ms time intervals the protein stability can be tested at different current densities. We investigated several proteins such as bovine and human serum albumins, ovalbumin, ot-macroglobulin and ot-synuclein, which showed various profiles in dependence

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Electrochimica acta

ISSN

0013-4686

e-ISSN

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Svazek periodika

174

Číslo periodika v rámci svazku

AUG 2015

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

5

Strana od-do

356-360

Kód UT WoS článku

000359873400044

EID výsledku v databázi Scopus

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