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Mass Spectrometry-Based Structural Analysis of Cysteine-Rich Metal-Binding Sites in Proteins with MetaOdysseus R Software

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F21%3A43918326" target="_blank" >RIV/62156489:43210/21:43918326 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216305:26620/21:PU137713

  • Result on the web

    <a href="https://doi.org/10.1021/acs.jproteome.0c00651" target="_blank" >https://doi.org/10.1021/acs.jproteome.0c00651</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acs.jproteome.0c00651" target="_blank" >10.1021/acs.jproteome.0c00651</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Mass Spectrometry-Based Structural Analysis of Cysteine-Rich Metal-Binding Sites in Proteins with MetaOdysseus R Software

  • Original language description

    Identification of metal-binding sites in proteins and understanding metal-coupled protein folding mechanisms are aspects of high importance for the structure-to-function relationship. Mass spectrometry (MS) has brought a powerful adjunct perspective to structural biology, obtaining from metal-to-protein stoichiometry to quaternary structure information. Currently, the different experimental and/or instrumental setups usually require the use of multiple data analysis software, and in some cases, they lack some of the main data analysis steps (MS processing, scoring, identification). Here, we present a comprehensive data analysis pipeline that addresses charge-state deconvolution, statistical scoring, and mass assignment for native MS, bottom-up, and native top-down with emphasis on metal-protein complexes. We have evaluated all of the approaches using assemblies of increasing complexity, including free and chemically labeled proteins, from low- to high-resolution MS. In all cases, the results have been compared with common software and proved how MetaOdysseus outperformed them.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10609 - Biochemical research methods

Result continuities

  • Project

    <a href="/en/project/LQ1601" target="_blank" >LQ1601: CEITEC 2020</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 Proteome Research

  • ISSN

    1535-3893

  • e-ISSN

  • Volume of the periodical

    20

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    776-785

  • UT code for WoS article

    000605145400068

  • EID of the result in the Scopus database

    2-s2.0-85098770896