Radical Reactions Affecting Polar Groups in Threonine Peptide Ions
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00477515" target="_blank" >RIV/61388963:_____/17:00477515 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1021/acs.jpcb.7b04661" target="_blank" >http://dx.doi.org/10.1021/acs.jpcb.7b04661</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.jpcb.7b04661" target="_blank" >10.1021/acs.jpcb.7b04661</a>
Alternative languages
Result language
angličtina
Original language name
Radical Reactions Affecting Polar Groups in Threonine Peptide Ions
Original language description
Peptide cation-radicals containing the threonine residue undergo radical induced dissociations upon collisional activation and photon absorption in the 210-400 nm range. Peptide cation-radicals containing a radical defect at the N-terminal residue, [(center dot)Ala-Thr-Ala-Arg+H](+), were generated by electron transfer dissociation (ETD) of peptide dications and characterized by UV vis photodissociation action spectroscopy combined with time-dependent density functional theory (TD-DFT) calculations of absorption spectra, including thermal vibronic band broadening. The acute spectrum of [(center dot)Ala-Thr-Ala-Arg+H](+) ions was indicative of the canonical structure of an N-terminally deaminated radical whereas isomeric structures differing in the position of the radical defect and amide bond geometry were excluded. This indicated that exothermic electron transfer to threonine peptide ions did not induce radical isomerizations in the fragment cation-radicals. Several isomeric structures, ion molecule complexes, and transition states for isomerizations and dissociations were generated and analyzed by DFT and Moller Plesset perturbational ab initio calculations to aid interpretation of the major dissociations by loss of water, hydroxyl radical, C3H6NO center dot, C3H7NO, and backbone cleavages. Born-Oppenheimer molecular dynamics (BOMD) in combination with DFT gradient geometry optimizations and intrinsic reaction coordinate analysis were used to search for low-energy cation-radical conformers and transition, states. BOMD was also employed to analyze the reaction trajectory for loss of water from ion molecule complexes.
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
10403 - Physical chemistry
Result continuities
Project
<a href="/en/project/GA17-24155S" target="_blank" >GA17-24155S: Exploring Conformational Space of Short Peptides by Advanced Quantum Chemical and Solvation Methods: A Key to Understand Protein Structures?</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2017
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 Physical Chemistry B
ISSN
1520-6106
e-ISSN
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Volume of the periodical
121
Issue of the periodical within the volume
27
Country of publishing house
US - UNITED STATES
Number of pages
13
Pages from-to
6557-6569
UT code for WoS article
000405764000012
EID of the result in the Scopus database
2-s2.0-85024928949