All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F21%3A00551051" target="_blank" >RIV/61388971:_____/21:00551051 - isvavai.cz</a>

  • Alternative codes found

    RIV/86652036:_____/21:00556422 RIV/61388963:_____/21:00551051 RIV/00216208:11310/21:10437999

  • Result on the web

    <a href="https://pubs.acs.org/doi/10.1021/jacs.1c07771" target="_blank" >https://pubs.acs.org/doi/10.1021/jacs.1c07771</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/jacs.1c07771" target="_blank" >10.1021/jacs.1c07771</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    Covalent 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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>SC</sub> - Article in a specialist periodical, which is included in the SCOPUS database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/GA19-16084S" target="_blank" >GA19-16084S: Mapping protein surface accessible area utilizing top-down mass spectrometry and reactive radical footprinting</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2021

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of the American Chemical Society

  • ISSN

    0002-7863

  • e-ISSN

    1520-5126

  • Volume of the periodical

    143

  • Issue of the periodical within the volume

    49

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    20670-20679

  • UT code for WoS article

    000750799000004

  • EID of the result in the Scopus database

    2-s2.0-85120891502