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Simple protein structure-sensitive chronopotentiometric analysis with dithiothreitol-modified Hg electrodes

  1. 1.
    SYSNO ASEP0383508
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleSimple protein structure-sensitive chronopotentiometric analysis with dithiothreitol-modified Hg electrodes
    Author(s) Ostatná, Veronika (BFU-R) RID, ORCID
    Černocká, Hana (BFU-R) RID, ORCID
    Paleček, Emil (BFU-R) RID, ORCID
    Number of authors3
    Source TitleBioelectrochemistry. - : Elsevier - ISSN 1567-5394
    Roč. 87, SI (2012), s. 84-88
    Number of pages5 s.
    Languageeng - English
    CountryNL - Netherlands
    Keywordsprotein electroanalysis ; DTT-modified electrodes ; electrocatalysis
    Subject RIVBO - Biophysics
    R&D ProjectsKJB100040901 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
    GAP301/11/2055 GA ČR - Czech Science Foundation (CSF)
    LC06035 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    CEZAV0Z50040507 - BFU-R (2005-2011)
    AV0Z50040702 - BFU-R (2007-2013)
    UT WOS000309033000014
    DOI10.1016/j.bioelechem.2012.01.004
    AnnotationIn the paper the authors studied the properties of the dithiothreitol (DTT) layer at the hanging mercury drop electrode. At higher DTT concentrations, a densely packed pinhole-free layer is formed with the DTT molecules bound to the electrode surface by a single -SH group, oriented perpendicularly to the surface. If a sufficiently high DTT concentration is used, proteins can be co-adsorbed with DTT on liquid Hg or solid amalgam electrodes without the loss of sensitivity for changes in protein structures.
    WorkplaceInstitute of Biophysics
    ContactJana Poláková, polakova@ibp.cz, Tel.: 541 517 244
    Year of Publishing2013
Number of the records: 1  

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