Influence of stereochemistry on proton transfer in protonated tripeptide models

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F12%3A00060043" target="_blank" >RIV/00216224:14740/12:00060043 - isvavai.cz</a>

Výsledek na webu

<a href="http://link.springer.com/article/10.1007%2Fs00894-011-1116-2" target="_blank" >http://link.springer.com/article/10.1007%2Fs00894-011-1116-2</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00894-011-1116-2" target="_blank" >10.1007/s00894-011-1116-2</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Influence of stereochemistry on proton transfer in protonated tripeptide models

Popis výsledku v původním jazyce

Vectorial proton transfer among carbonyl oxygen atoms was studied in two models of tripeptide via quantum chemical calculations using the hybrid B3LYP functional and the 6-31++G** basis set. Two principal proton transfer pathways were found: a first pathinvolving isomerization of the proton around the double bond of the carbonyl group, and a second based on the large conformational flexibility of the tripeptide model where all carbonyl oxygen atoms cooperate. The latter pathway has a rate-determining step energy barrier that is only around half of that for the first pathway. As conformational flexibility plays a crucial role in second pathway, the effect of attaching methyl groups to the alpha carbon atoms was studied. The results obtained are presented for all four possible stereochemical configurations.

Název v anglickém jazyce

Influence of stereochemistry on proton transfer in protonated tripeptide models

Popis výsledku anglicky

Vectorial proton transfer among carbonyl oxygen atoms was studied in two models of tripeptide via quantum chemical calculations using the hybrid B3LYP functional and the 6-31++G** basis set. Two principal proton transfer pathways were found: a first pathinvolving isomerization of the proton around the double bond of the carbonyl group, and a second based on the large conformational flexibility of the tripeptide model where all carbonyl oxygen atoms cooperate. The latter pathway has a rate-determining step energy barrier that is only around half of that for the first pathway. As conformational flexibility plays a crucial role in second pathway, the effect of attaching methyl groups to the alpha carbon atoms was studied. The results obtained are presented for all four possible stereochemical configurations.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/LC06030" target="_blank" >LC06030: Biomolekulární centrum</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

—

Svazek periodika

18

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

871-879

Kód UT WoS článku

000303539500005

EID výsledku v databázi Scopus

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