Glycosyltransferase LgtC: MD Simulations under Physiological and Non-physiological Conditions

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F04%3A00010546" target="_blank" >RIV/00216224:14310/04:00010546 - 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

Glycosyltransferasa LgtC: MD Simulace

Popis výsledku v původním jazyce

First molecular dynamics (MD) simulations, performed on complex LgtC with manganese ion and donor substrate (UDP-Gal), were recently reported [3]. Since the amino acid sequence in the crystal structure is shorter than that in natural enzyme (29 residuesin C-terminal domain missing), the artificial carboxyl group on C-terminal (Leu282) was considered in that study. In this work, we have run several MD simulations of systems with blocked (electro-neutral Nmethylamide.) and native Leu282 and have comparedthe results. We have also focused our attention on analysis of behavior of this enzyme under physiological and non-physiological conditions during the MD simulations. Even if physiological conditions (0.1 M NaCl) are more natural for proteins, they arenot frequently used in computational methods as the presence of relatively high concentration of ions may cause problems. We will show differences in behaviour of the protein with blocked and native C-terminal carboxyl group, and of syste

Název v anglickém jazyce

Glycosyltransferasa LgtC: MD Simulace

Popis výsledku anglicky

First molecular dynamics (MD) simulations, performed on complex LgtC with manganese ion and donor substrate (UDP-Gal), were recently reported [3]. Since the amino acid sequence in the crystal structure is shorter than that in natural enzyme (29 residuesin C-terminal domain missing), the artificial carboxyl group on C-terminal (Leu282) was considered in that study. In this work, we have run several MD simulations of systems with blocked (electro-neutral Nmethylamide.) and native Leu282 and have comparedthe results. We have also focused our attention on analysis of behavior of this enzyme under physiological and non-physiological conditions during the MD simulations. Even if physiological conditions (0.1 M NaCl) are more natural for proteins, they arenot frequently used in computational methods as the presence of relatively high concentration of ions may cause problems. We will show differences in behaviour of the protein with blocked and native C-terminal carboxyl group, and of syste

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název statě ve sborníku

22nd International Carbohydrate Symposium

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

"P388"

Název nakladatele

International Carbohydrate Organisation

Místo vydání

Glasgow

Místo konání akce

Glasgow, Great Britain

Datum konání akce

1. 1. 2004

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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