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%2F00216305%3A26620%2F21%3APU137713" target="_blank" >RIV/00216305:26620/21:PU137713 - isvavai.cz</a>
Alternative codes found
RIV/62156489:43210/21:43918326
Result on the web
<a href="https://pubs.acs.org/doi/10.1021/acs.jproteome.0c00651" target="_blank" >https://pubs.acs.org/doi/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 metalcoupled protein folding mechanisms are aspects of high importance for the structure-tofunction 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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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
1535-3907
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
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