Počet záznamů: 1  

Fast Fluoroalkylation of Proteins Uncovers the Structure and Dynamics of Biological Macromolecules

  1. 1.
    SYSNO ASEP0556422
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevFast Fluoroalkylation of Proteins Uncovers the Structure and Dynamics of Biological Macromolecules
    Tvůrce(i) Fojtik, L. (CZ)
    Fiala, J. (CZ)
    Pompach, Petr (BTO-N)
    Chmelík, J. (CZ)
    Matoušek, V. (CZ)
    Beier, P. (CZ)
    Kukačka, Z. (CZ)
    Novák, P. (CZ)
    Celkový počet autorů8
    Zdroj.dok.Journal of the American Chemical Society. - : American Chemical Society - ISSN 0002-7863
    Roč. 143, č. 49 (2021), s. 20670-20679
    Poč.str.10 s.
    Jazyk dok.eng - angličtina
    Země vyd.US - Spojené státy americké
    Klíč. slovafast photochemical oxidation ; hypervalent iodine reagents ; mass-spectrometry ; top-down ; myoglobin
    Vědní obor RIVCB - Analytická chemie, separace
    Obor OECDAnalytical chemistry
    Způsob publikováníOpen access
    Institucionální podporaBTO-N - RVO:86652036
    UT WOS000750799000004
    EID SCOPUS85120891502
    DOI10.1021/jacs.1c07771
    AnotaceCovalent labeling of proteins in combination with mass spectrometry has been established as a complementary technique to classical structural methods, such as X-ray, NMR, or cryogenic electron microscopy (Cryo-EM), used for protein structure determination. Although the current covalent labeling techniques enable the protein solvent accessible areas with sufficient spatial resolution to be monitored, there is still high demand for alternative, less complicated, and inexpensive approaches. Here, we introduce a new covalent labeling method based on fast fluoroalkylation of proteins (FFAP). FFAP uses fluoroalkyl radicals formed by reductive decomposition of Togni reagents with ascorbic acid to label proteins on a time scale of seconds. The feasibility of FFAP to effectively label proteins was demonstrated by monitoring the differential amino acids modification of native horse heart apomyoglobin/holomyoglobin and the human haptoglobin-hemoglobin complex. The obtained data confirmed the Togni reagent-mediated FFAP is an advantageous alternative method for covalent labeling in applications such as protein footprinting and epitope mapping of proteins (and their complexes) in general. Data are accessible via the ProteomeXchange server with the data set identifier PXD027310.
    PracovištěBiotechnologický ústav
    KontaktMonika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700
    Rok sběru2022
    Elektronická adresahttps://pubs.acs.org/doi/10.1021/jacs.1c07771
Počet záznamů: 1  

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