Počet záznamů: 1
Voltammetric and chronopotentiometric protein structure-sensitive analysis
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SYSNO ASEP 0471362 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Voltammetric and chronopotentiometric protein structure-sensitive analysis Tvůrce(i) Černocká, Hana (BFU-R) RID, ORCID
Paleček, Emil (BFU-R) RID, ORCIDCelkový počet autorů 2 Zdroj.dok. Electrochimica acta. - : Elsevier - ISSN 0013-4686
Roč. 224, JAN2017 (2017), s. 211-219Poč.str. 9 s. Forma vydání Tištěná - P Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova circular-dichroism spectroscopy ; catalytic hydrogen evolution ; mercury-electrodes Vědní obor RIV BO - Biofyzika CEP GA15-15479S GA ČR - Grantová agentura ČR Institucionální podpora BFU-R - RVO:68081707 UT WOS 000392165800026 DOI 10.1016/j.electacta.2016.12.047 Anotace Previously we showed that constant current chronopotentiometric stripping (CPS) is convenient for protein analysis based on the ability of some amino acid residues to catalyze hydrogen evolution on mercury-containing electrodes. This method showed a remarkable sensitivity to changes in protein structures, including protein denaturation and even small protein damage. Here we used normal pulse voltammetric stripping (NPVS) with bare and dithiothreitol-modified hanging mercury drop electrode. We found that NPV pulses denatured the surface-attached protein but we showed conditions under which this method was able to distinguish native and denatured proteins with sensitivity approaching that of CPS. Using NPVS it was possible to follow bovine serum albumin (BSA) thermal denaturation as well as to investigate the effect of NPV pulses on the structure of the surface-attached protein. In addition to BSA we studied several proteins, such as human serum albumin, ovalbumin, urease, aldolase, concanavalin A, histone and vasopressin peptide. Our results suggest that CPS remains the method-of choice for studies of changes in protein structure and of biochemical processes, such as DNA-protein specific binding, lectin-glycoprotein interactions, detection of protein damage, etc., while voltammetric methods, such as NPVS may suit better for investigation of the processes which proteins undergo at the electrode surface. (C) 2016 Elsevier Ltd. All rights reserved. Pracoviště Biofyzikální ústav Kontakt Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Rok sběru 2017
Počet záznamů: 1