Benefits of Ion Mobility Separation and Parallel
Accumulation-Serial Fragmentation Technology on timsTOF Pro for
the Needs of Fast Photochemical Oxidation of Protein Analysis

J 2021

Benefits of Ion Mobility Separation and Parallel Accumulation-Serial Fragmentation Technology on timsTOF Pro for the Needs of Fast Photochemical Oxidation of Protein Analysis

LOGINOV, D.S., J. FIALA, J. CHMELIK, P. BRECHLIN, G. KRUPPA et. al.

Základní údaje

Originální název

Benefits of Ion Mobility Separation and Parallel Accumulation-Serial Fragmentation Technology on timsTOF Pro for the Needs of Fast Photochemical Oxidation of Protein Analysis

Autoři

LOGINOV, D.S., J. FIALA, J. CHMELIK, P. BRECHLIN, G. KRUPPA a P. NOVAK

Vydání

ACS OMEGA, 2021, 2470-1343

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10400 1.4 Chemical sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.132

Kód RIV

RIV/00216224:14740/21:00124532

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1021/acsomega.1c00732

UT WoS

000643537100037

Klíčová slova anglicky

Peptide Mapping; Hydrogen Deuterium Exchange-Mass Spectrometry; Glycine Ethyl Ester

Štítky

ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 18. 5. 2022 15:02, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

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

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

LOGINOV, D.S., J. FIALA, J. CHMELIK, P. BRECHLIN, G. KRUPPA a P. NOVAK. Benefits of Ion Mobility Separation and Parallel Accumulation-Serial Fragmentation Technology on timsTOF Pro for the Needs of Fast Photochemical Oxidation of Protein Analysis. ACS OMEGA. 2021, roč. 6, č. 15, s. 10352-10361. ISSN 2470-1343. Dostupné z: https://dx.doi.org/10.1021/acsomega.1c00732.

@article{1846842,
   author = {Loginov, D.S. and Fiala, J. and Chmelik, J. and Brechlin, P. and Kruppa, G. and Novak, P.},
   article_number = {15},
   doi = {http://dx.doi.org/10.1021/acsomega.1c00732},
   keywords = {Peptide Mapping; Hydrogen Deuterium Exchange-Mass Spectrometry; Glycine Ethyl Ester},
   language = {eng},
   issn = {2470-1343},
   journal = {ACS OMEGA},
   title = {Benefits of Ion Mobility Separation and Parallel Accumulation-Serial Fragmentation Technology on timsTOF Pro for the Needs of Fast Photochemical Oxidation of Protein Analysis},
   url = {https://pubs.acs.org/doi/10.1021/acsomega.1c00732},
   volume = {6},
   year = {2021}
}

TY  - JOUR
ID  - 1846842
AU  - Loginov, D.S. - Fiala, J. - Chmelik, J. - Brechlin, P. - Kruppa, G. - Novak, P.
PY  - 2021
TI  - Benefits of Ion Mobility Separation and Parallel Accumulation-Serial Fragmentation Technology on timsTOF Pro for the Needs of Fast Photochemical Oxidation of Protein Analysis
JF  - ACS OMEGA
VL  - 6
IS  - 15
SP  - 10352-10361
EP  - 10352-10361
SN  - 24701343
KW  - Peptide Mapping
KW  - Hydrogen Deuterium Exchange-Mass Spectrometry
KW  - Glycine Ethyl Ester
UR  - https://pubs.acs.org/doi/10.1021/acsomega.1c00732
N2  - 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
ER  -

LOGINOV, D.S., J. FIALA, J. CHMELIK, P. BRECHLIN, G. KRUPPA a P. NOVAK. Benefits of Ion Mobility Separation and Parallel Accumulation-Serial Fragmentation Technology on timsTOF Pro for the Needs of Fast Photochemical Oxidation of Protein Analysis. \textit{ACS OMEGA}. 2021, roč.~6, č.~15, s.~10352-10361. ISSN~2470-1343. Dostupné z: https://dx.doi.org/10.1021/acsomega.1c00732.

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