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

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About: Homology Modelling and Molecular Dynamics Simulation of Beta-Galactosidase from Antarctic Bacterium Arthrobacter sp. C2-2 - sborník Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	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 are discussed. 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 are discussed. (en)
Title	Homology Modelling and Molecular Dynamics Simulation of Beta-Galactosidase from Antarctic Bacterium Arthrobacter sp. C2-2 - sborník Homology Modelling and Molecular Dynamics Simulation of Beta-Galactosidase from Antarctic Bacterium Arthrobacter sp. C2-2 - sborník (en)
skos:prefLabel	Homology Modelling and Molecular Dynamics Simulation of Beta-Galactosidase from Antarctic Bacterium Arthrobacter sp. C2-2 - sborník Homology Modelling and Molecular Dynamics Simulation of Beta-Galactosidase from Antarctic Bacterium Arthrobacter sp. C2-2 - sborník (en)
skos:notation	RIV/60461373:22330/03:00008977!RIV/2004/GA0/223304/N
http://linked.open.../vavai/riv/strany	763
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(GA204/02/0843)
http://linked.open...vai/riv/dodaniDat	2004
http://linked.open...aciTvurceVysledku	Lipovová, Petra Spiwok, Vojtěch Strnad, Hynek Králová, Blanka
http://linked.open.../riv/druhVysledku	D - Článek ve sborníku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Vysoká škola chemicko-technologická v Praze / Fakulta potravinářské a biochemické technologie
http://linked.open...dnocenehoVysledku	609284
http://linked.open...ai/riv/idVysledku	RIV/60461373:22330/03:00008977
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Cold-active enzyme (en)
http://linked.open.../riv/klicoveSlovo	Cold-active enzyme
http://linked.open...ontrolniKodProRIV	[32B765AAEDDB]
http://linked.open...v/mistoKonaniAkce	Montreal
http://linked.open...i/riv/mistoVydani	Bethesda
http://linked.open...i/riv/nazevZdroje	Molecular & Cellular Proteomics
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	4 (xsd:int)
http://linked.open...cetTvurcuVysledku	4 (xsd:int)
http://linked.open...ocetUcastnikuAkce	0 (xsd:int)
http://linked.open...nichUcastnikuAkce	0 (xsd:int)
http://linked.open...vavai/riv/projekt	Complex cold adaptation study of enzymes on molecular level and their application in biotechnology
http://linked.open...UplatneniVysledku	2003
http://linked.open...iv/tvurceVysledku	Spiwok, Vojtěch Strnad, Hynek Králová, Blanka Karasová, Petra
http://linked.open...vavai/riv/typAkce	WRD - Světová
http://linked.open.../riv/zahajeniAkce	2003-09-08 (xsd:date)
issn	1535-9476
number of pages	1 (xsd:int)
http://purl.org/ne...btex#hasPublisher	American Society for Biochemistry and Molecular Biology
http://localhost/t...ganizacniJednotka	22330

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