About: Beta-Galactosidase from Antarctic bacterium Arthrobacter sp. C2-2: a molecular modelling study

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About: Beta-Galactosidase from Antarctic bacterium Arthrobacter sp. C2-2: a molecular modelling study 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 microorganisms are being studied as potential catalysts in biotechnology as well as models of adaptation on an evolutionary level. The relationship between structural features of these enzymes and their ability to efficiently catalyse reactions at low temperatures is not clear. A study of beta-galactosidase from Antarctic bacteria Arthrobacter sp. C2-2 is presented. Model of 3D-structure of this enzyme was built using a methodology of homology modelling by satisfaction of spatial restraints based on structure of beta-galactosidase from E. coli (1DP0), the structure of one loop region was predicted ab initio. Interactions between the enzyme and ligands (galactose, water and ions) was studied using a methodology of molecular fields, docking, molecular dynamics simulation and free-energy scoring. Overall quality of the model was evaluated by 1 ns molecular dynamics simulation. We present comparison of structural features of the studied enzyme and its mesophilic counterpart from Enzymes from cold adapted microorganisms are being studied as potential catalysts in biotechnology as well as models of adaptation on an evolutionary level. The relationship between structural features of these enzymes and their ability to efficiently catalyse reactions at low temperatures is not clear. A study of beta-galactosidase from Antarctic bacteria Arthrobacter sp. C2-2 is presented. Model of 3D-structure of this enzyme was built using a methodology of homology modelling by satisfaction of spatial restraints based on structure of beta-galactosidase from E. coli (1DP0), the structure of one loop region was predicted ab initio. Interactions between the enzyme and ligands (galactose, water and ions) was studied using a methodology of molecular fields, docking, molecular dynamics simulation and free-energy scoring. Overall quality of the model was evaluated by 1 ns molecular dynamics simulation. We present comparison of structural features of the studied enzyme and its mesophilic counterpart from (en)
Title	Beta-Galactosidase from Antarctic bacterium Arthrobacter sp. C2-2: a molecular modelling study Beta-Galactosidase from Antarctic bacterium Arthrobacter sp. C2-2: a molecular modelling study (en)
skos:prefLabel	Beta-Galactosidase from Antarctic bacterium Arthrobacter sp. C2-2: a molecular modelling study Beta-Galactosidase from Antarctic bacterium Arthrobacter sp. C2-2: a molecular modelling study (en)
skos:notation	RIV/60461373:22330/03:00008978!RIV/2004/GA0/223304/N
http://linked.open.../vavai/riv/strany	14
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 Malá, Šárka 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	599656
http://linked.open...ai/riv/idVysledku	RIV/60461373:22330/03:00008978
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Psychrotrophic microorganisms (en)
http://linked.open.../riv/klicoveSlovo	Psychrotrophic microorganisms
http://linked.open...ontrolniKodProRIV	[04C62C69B813]
http://linked.open...v/mistoKonaniAkce	Praha
http://linked.open...i/riv/mistoVydani	Praha
http://linked.open...i/riv/nazevZdroje	Sborník CUKRBLIK
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	5 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (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 Malá, Šárka Karasová, Petra
http://linked.open...vavai/riv/typAkce	CST - Celostátní
http://linked.open.../riv/zahajeniAkce	2003-04-16 (xsd:date)
number of pages	1 (xsd:int)
http://purl.org/ne...btex#hasPublisher	Vysoká škola chemicko-technologická v Praze
https://schema.org/isbn	80-86238-30-2
http://localhost/t...ganizacniJednotka	22330

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