Conformational free energy surface of a-N-acetylneuraminic acid: An interplay between hydrogen bonding and solvation.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F09%3A00022337" target="_blank" >RIV/60461373:22330/09:00022337 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Conformational free energy surface of a-N-acetylneuraminic acid: An interplay between hydrogen bonding and solvation.

Popis výsledku v původním jazyce

The conformational free energy surface of alpha-N-acetylneuraminic acid (Neu5Ac, sialic acid) in the space of ring-puckering coordinates was calculated using the metadynamics method. Free energy surfaces in vacuum and with an explicit solvent were calculated in GLYCAM 06 force field. In vacuum three structures are almost equivalently populated, namely, the 2C5 chair and the B3,6/2S6 and OS3 boat/skew-boat conformations. The B3,6/2S6 structure is stabilized by an ionic hydrogen bond between the amide N-Hbond and the carboxylic group. However, this structure is unfavorable in a water environment in which the experimentally observed 2C5 chair conformation is predicted to be more stable than the other structures. These results indicate that environment significantly influences conformation of Neu5Ac and that Neu5Ac-processing enzymes might modify a conformation of their substrates solely by a changing polarity of the environment. The structure of Neu5Ac bound in influenza neuraminidase (4

Název v anglickém jazyce

Conformational free energy surface of a-N-acetylneuraminic acid: An interplay between hydrogen bonding and solvation.

Popis výsledku anglicky

The conformational free energy surface of alpha-N-acetylneuraminic acid (Neu5Ac, sialic acid) in the space of ring-puckering coordinates was calculated using the metadynamics method. Free energy surfaces in vacuum and with an explicit solvent were calculated in GLYCAM 06 force field. In vacuum three structures are almost equivalently populated, namely, the 2C5 chair and the B3,6/2S6 and OS3 boat/skew-boat conformations. The B3,6/2S6 structure is stabilized by an ionic hydrogen bond between the amide N-Hbond and the carboxylic group. However, this structure is unfavorable in a water environment in which the experimentally observed 2C5 chair conformation is predicted to be more stable than the other structures. These results indicate that environment significantly influences conformation of Neu5Ac and that Neu5Ac-processing enzymes might modify a conformation of their substrates solely by a changing polarity of the environment. The structure of Neu5Ac bound in influenza neuraminidase (4

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2009

Kód důvěrnosti údajů

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

Název periodika

JOURNAL OF PHYSICAL CHEMISTRY B

ISSN

1520-6106

e-ISSN

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Svazek periodika

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Číslo periodika v rámci svazku

113

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

6

Strana od-do

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Kód UT WoS článku

000268139000033

EID výsledku v databázi Scopus

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