Benefits of Ion Mobility Separation and Parallel Accumulation-Serial Fragmentation Technology on timsTOF Pro for the Needs of Fast Photochemical Oxidation of Protein Analysis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A90127%2F21%3A00139999" target="_blank" >RIV/00216224:90127/21:00139999 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/21:00543515 RIV/00216208:11310/21:10430213
Result on the web
<a href="https://pubs.acs.org/doi/10.1021/acsomega.1c00732" target="_blank" >https://pubs.acs.org/doi/10.1021/acsomega.1c00732</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acsomega.1c00732" target="_blank" >10.1021/acsomega.1c00732</a>
Alternative languages
Result language
angličtina
Original language name
Benefits of Ion Mobility Separation and Parallel Accumulation-Serial Fragmentation Technology on timsTOF Pro for the Needs of Fast Photochemical Oxidation of Protein Analysis
Original language description
Fast photochemical oxidation of proteins (FPOP) is a recently developed technique for studying protein folding, conformations, interactions, etc. In this method, hydroxyl radicals, usually generated by KrF laser photolysis of H2O2, are used for irreversible labeling of solvent-exposed side chains of amino acids. Mapping of the oxidized residues to the protein's structure requires pinpointing of modifications using a bottom-up proteomic approach. In this work, a quadrupole time-of-flight (QTOF) mass spectrometer coupled with trapped ion mobility spectrometry (timsTOF Pro) was used for identification of oxidative modifications in a model protein. Multiple modifications on the same residues, including six modifications of histidine, were successfully resolved. Moreover, parallel accumulation-serial fragmentation (PASEF) technology allows successful sequencing of even minor populations of modified peptides. The data obtained indicate a clear improvement of the quality of the FPOP analysis from the viewpoint of the number of identified peptides bearing oxidative modifications and their precise localization. Data are available via ProteomeXchange with identifier
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
10400 - Chemical sciences
Result continuities
Project
—
Continuities
—
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
ACS OMEGA
ISSN
2470-1343
e-ISSN
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Volume of the periodical
6
Issue of the periodical within the volume
15
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
10352-10361
UT code for WoS article
000643537100037
EID of the result in the Scopus database
2-s2.0-85105056799