About: Role of CH/pi interactions in substrate binding by Escherichia coli ß-galactosidase

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Interactions between carbohydrates and aromatic amino-acid residues are often observed in structures of carbohydrate-protein complexes. They are characterized by an orientation of the pyranose or furanose ring parallel with the aromatic ring of amino-acid residues. An important role in the formation of these complexes is supposed to be played by CH/pi interactions. This paper presents an ab initio quantum chemistry study of CH/pi interactions between beta-galactosidase from E. coli and its substrates and products. The energy stabilizing the interaction between Trp999 residue and substrate bound in the shallow binding mode was calculated at the MP2/6-31+G(d) level as 5.2kcalmol(-1) for the glucose moiety of allolactose, 2.4kcalmol(-1) for the galactose moiety of allolactose and 5.0kcalmol(-1) for the glucose moiety of lactose. The energy stabilizing the interaction between Trp568 residue and galactose in the deep binding mode was calculated as 2.7kcalmol(-1). Interaction energies at the HF/6-31+G(d) an Interactions between carbohydrates and aromatic amino-acid residues are often observed in structures of carbohydrate-protein complexes. They are characterized by an orientation of the pyranose or furanose ring parallel with the aromatic ring of amino-acid residues. An important role in the formation of these complexes is supposed to be played by CH/pi interactions. This paper presents an ab initio quantum chemistry study of CH/pi interactions between beta-galactosidase from E. coli and its substrates and products. The energy stabilizing the interaction between Trp999 residue and substrate bound in the shallow binding mode was calculated at the MP2/6-31+G(d) level as 5.2kcalmol(-1) for the glucose moiety of allolactose, 2.4kcalmol(-1) for the galactose moiety of allolactose and 5.0kcalmol(-1) for the glucose moiety of lactose. The energy stabilizing the interaction between Trp568 residue and galactose in the deep binding mode was calculated as 2.7kcalmol(-1). Interaction energies at the HF/6-31+G(d) an (en) Úloha CH/pi interakcí při vazbě substrátu v ß-galaktosidase z Escherichia coli (cs)
Title	Role of CH/pi interactions in substrate binding by Escherichia coli ß-galactosidase Role of CH/pi interactions in substrate binding by Escherichia coli ß-galactosidase (en) Úloha CH/pi interakcí při vazbě substrátu v ß-galaktosidase z Escherichia coli (cs)
skos:prefLabel	Role of CH/pi interactions in substrate binding by Escherichia coli ß-galactosidase Role of CH/pi interactions in substrate binding by Escherichia coli ß-galactosidase (en) Úloha CH/pi interakcí při vazbě substrátu v ß-galaktosidase z Escherichia coli (cs)
skos:notation	RIV/60461373:22330/04:00012882!RIV/2005/GA0/223305/N
http://linked.open.../vavai/riv/strany	2275-2280
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA204/02/0843), Z(MSM 223300006)
http://linked.open...iv/cisloPeriodika	13
http://linked.open...vai/riv/dodaniDat	2005
http://linked.open...aciTvurceVysledku	Lipovová, Petra Spiwok, Vojtěch Králová, Blanka
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
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	584944
http://linked.open...ai/riv/idVysledku	RIV/60461373:22330/04:00012882
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Molecular recognition (en)
http://linked.open.../riv/klicoveSlovo	Molecular recognition
http://linked.open...odStatuVydavatele	BE - Belgické království
http://linked.open...ontrolniKodProRIV	[1035A1F28996]
http://linked.open...i/riv/nazevZdroje	Carbohydrate Research
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	6 (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	2004
http://linked.open...v/svazekPeriodika	339
http://linked.open...iv/tvurceVysledku	Hašek, Jindřich Skálová, Tereza Spiwok, Vojtěch Králová, Blanka Buchtelová, Eva Karasová, Petra
http://linked.open...n/vavai/riv/zamer	http://linked.opendata.cz/resource/domain/vavai/zamer/MSM%20223300006
issn	0008-6215
number of pages	5 (xsd:int)
http://localhost/t...ganizacniJednotka	22330

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