0546664 - BFÚ 2022 RIV DE eng J - Journal Article
Melnikova, E. - Galicová, Tatiana - Gál, M. - Ostatná, Veronika
Chronopotentiometric Analysis of Single Histones and Histone Octamer at Charged Surfaces.
ChemElectroChem. Roč. 8, č. 17 (2021), s. 3360-3365. ISSN 2196-0216. E-ISSN 2196-0216
Institutional support: RVO:68081707
Keywords : catalyzed hydrogen evolution * electrochemistry * adsorption * proteins
OECD category: Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)
Impact factor: 4.782, year: 2021 ; AIS: 0.744, rok: 2021
Method of publishing: Limited access
Result website:
https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/celc.202100817DOI: https://doi.org/10.1002/celc.202100817

Histones play an essential role in the nucleosome structure and organization. The key role of highly positively charged histones is to stabilize negatively charged DNA inside the chromatin. Histones are basic proteins containing a large amount of electroactive residues, namely, arginine and lysine. Additionally, histone H3, on the contrary to other histones, contains cysteine residues. To understand more about the behavior of histones at charged surfaces and the influence of the electroactive amino acid residues content on the catalytic hydrogen evolution reaction, we studied histones using label-free approaches, namely, chronopotentiometric stripping analysis (CPS) and impedance C-d-t curves. While CPS is sensitive to the structure and stability of proteins and their complexes, C-d-t curves reflect changes of the electrical double layer at the charged surface. Application of both label-free methods appears useful for analysis of complex systems. Using a combination of these methods, we could discriminate between individual single core histones, their mixture, and their complex (octamer).
Permanent Link: http://hdl.handle.net/11104/0323089