Homology Modelling and Molecular Dynamics Simulation of Beta-Galactosidase from Antarctic Bacterium Arthrobacter sp. C2-2 - sborník

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F03%3A00008977" target="_blank" >RIV/60461373:22330/03:00008977 - 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

Homology Modelling and Molecular Dynamics Simulation of Beta-Galactosidase from Antarctic Bacterium Arthrobacter sp. C2-2 - sborník

Popis výsledku v původním jazyce

Enzymes from cold adapted organisms are gaining interest as catalysts in biotechnology. b­Galactosidase from Antarctic bacterium Arthrobacter sp. C2 ­2 was used as a model enzyme to study the structural b asis of adaptation to function at low temperature. Since the experimental structure is not yet known we used methodology of homology modelling and molecular dynamics simulation. Model was built by the method of homology modelling by satisfaction of spatial restraints. b­Galactosidase from E.coli (PDB identifier 1DP0) and human b­glucuronidase (PDB identifier 1BHG) were used as templates. To evaluate and optimize the model, homology modelling procedure was followed by simulation of 1 ns molecular dynamics. Presented work describes results of moleculardynamics simulation and their implication for understanding of mechanism of adaptation . Predicted structure of the enzyme is compared with its mesophilic counterpart and roles of electrostatic and hydrophobic interactions in adaptation ar

Název v anglickém jazyce

Homology Modelling and Molecular Dynamics Simulation of Beta-Galactosidase from Antarctic Bacterium Arthrobacter sp. C2-2 - sborník

Popis výsledku anglicky

Enzymes from cold adapted organisms are gaining interest as catalysts in biotechnology. b­Galactosidase from Antarctic bacterium Arthrobacter sp. C2 ­2 was used as a model enzyme to study the structural b asis of adaptation to function at low temperature. Since the experimental structure is not yet known we used methodology of homology modelling and molecular dynamics simulation. Model was built by the method of homology modelling by satisfaction of spatial restraints. b­Galactosidase from E.coli (PDB identifier 1DP0) and human b­glucuronidase (PDB identifier 1BHG) were used as templates. To evaluate and optimize the model, homology modelling procedure was followed by simulation of 1 ns molecular dynamics. Presented work describes results of moleculardynamics simulation and their implication for understanding of mechanism of adaptation . Predicted structure of the enzyme is compared with its mesophilic counterpart and roles of electrostatic and hydrophobic interactions in adaptation ar

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA204%2F02%2F0843" target="_blank" >GA204/02/0843: Komplexní studium chladového přizpůsobení enzymů na molekulární úrovni a jejich uplatnění v biotechnologických procesech</a><br>

Návaznosti

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

Rok uplatnění

2003

Kód důvěrnosti údajů

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

Název statě ve sborníku

Molecular & Cellular Proteomics

ISBN

1535-9476

ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

763

Název nakladatele

American Society for Biochemistry and Molecular Biology

Místo vydání

Bethesda

Místo konání akce

Montreal

Datum konání akce

8. 9. 2003

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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