Chronopotentiometric Analysis of Proteins at Charged Electrode Surfaces

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F19%3A00511687" target="_blank" >RIV/68081707:_____/19:00511687 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14310/19:00113460

Výsledek na webu

<a href="https://onlinelibrary.wiley.com/doi/full/10.1002/elan.201900239" target="_blank" >https://onlinelibrary.wiley.com/doi/full/10.1002/elan.201900239</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/elan.201900239" target="_blank" >10.1002/elan.201900239</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Chronopotentiometric Analysis of Proteins at Charged Electrode Surfaces

Popis výsledku v původním jazyce

Protein properties and functions are strongly dependent on the structure and amino acid content. In this work, catalytic hydrogen evolution reaction (CHER) of five proteins (human serum albumin, lysozyme, beta-synuclein, H2 A and H3 histones) were studied using constant current chronopotentiometric stripping (CPS) with the aim to find out the association between protein content and its electrochemical response. We have shown that the height and potential of CPS peak H in dependence on accumulation potential differed for the studied proteins, while the CPS peak area was almost the same for all of them. CV and CPS peaks H of Cys-containing proteins appeared at less negative potentials in comparison to proteins without Cys, suggesting easier CHER. Acidic and basic proteins not containing Cys can be also recognized due to their different CPS response after their adsorption at the positive and negative charged interface.

Název v anglickém jazyce

Chronopotentiometric Analysis of Proteins at Charged Electrode Surfaces

Popis výsledku anglicky

Protein properties and functions are strongly dependent on the structure and amino acid content. In this work, catalytic hydrogen evolution reaction (CHER) of five proteins (human serum albumin, lysozyme, beta-synuclein, H2 A and H3 histones) were studied using constant current chronopotentiometric stripping (CPS) with the aim to find out the association between protein content and its electrochemical response. We have shown that the height and potential of CPS peak H in dependence on accumulation potential differed for the studied proteins, while the CPS peak area was almost the same for all of them. CV and CPS peaks H of Cys-containing proteins appeared at less negative potentials in comparison to proteins without Cys, suggesting easier CHER. Acidic and basic proteins not containing Cys can be also recognized due to their different CPS response after their adsorption at the positive and negative charged interface.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

Electroanalysis

ISSN

1040-0397

e-ISSN

—

Svazek periodika

31

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

5

Strana od-do

1868-1872

Kód UT WoS článku

000491476600004

EID výsledku v databázi Scopus

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