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Fast-scan cyclic voltammetry with thiol-modified mercury electrodes distinguishes native from denatured BSA
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SYSNO ASEP 0472036 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Fast-scan cyclic voltammetry with thiol-modified mercury electrodes distinguishes native from denatured BSA Author(s) Černocká, Hana (BFU-R) RID, ORCID
Ostatná, Veronika (BFU-R) RID, ORCID
Paleček, Emil (BFU-R) RID, ORCIDNumber of authors 3 Source Title Electrochemistry Communications. - : Elsevier - ISSN 1388-2481
Roč. 61, DEC2015 (2015), s. 114-116Number of pages 3 s. Publication form Print - P Language eng - English Country NL - Netherlands Keywords catalyzed hydrogen evolution ; proteins ; electrocatalysis Subject RIV BO - Biophysics R&D Projects GA15-15479S GA ČR - Czech Science Foundation (CSF) Institutional support BFU-R - RVO:68081707 UT WOS 000367124900027 DOI 10.1016/j.elecom.2015.10.017 Annotation We studied native and denatured bovine serum albumin (BSA) at bare and dithiothreithol (DTT)-modified hanging mercury drop electrode (HMDE) by fast-scan cyclic voltammetry (fsCV) and chronopotentiometric stripping (CPS) to compare these methods for their ability to recognize changes in BSA structure. Using fsCV and bare HMDE, denatured BSA could be distinguished from its native form only between 10 and 20 V/s but at lower resolution than with CPS. At DTT-HMDE denatured BSA was recognized from native BSA in a wider range of scan rates suggesting new possibilities in development of voltammetric protein structure-sensitive sensing. (C) 2015 Elsevier B.V. All rights reserved. Workplace Institute of Biophysics Contact Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Year of Publishing 2017
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