About: pKa Calculation for Selected Active Site Residues in Acetylcholinesterase

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Acetylcholinesterase (AChE) is a vitally important enzyme participating in nerve signal transmission connected with Alzheimer disease and nerve agent poisoning. Molecular dynamics simulations in the Amber force field 03 have revealed large conformational changes of the omega loop (Cys69 – Cys96 in 2HA2 crystal structure) occurring when AChE is in its deprotonated state [1]. According to the ff03 MD results, the omega loop dynamics is dependent of the protonation of active site residues, namely Glu202, Glu334, Glu450 (numbering of 2HA2). Simulations of the protonated AChE show much more stable and less mobile omega loop and Trp86. Such omega loop conformations are not seen in any of the crystal structures of AChE. Furthermore, a great deal of experimental evidence disproves that larger conformational rearrangements of omega loop would take part in the reaction mechanism [2]. Acetylcholinesterase (AChE) is a vitally important enzyme participating in nerve signal transmission connected with Alzheimer disease and nerve agent poisoning. Molecular dynamics simulations in the Amber force field 03 have revealed large conformational changes of the omega loop (Cys69 – Cys96 in 2HA2 crystal structure) occurring when AChE is in its deprotonated state [1]. According to the ff03 MD results, the omega loop dynamics is dependent of the protonation of active site residues, namely Glu202, Glu334, Glu450 (numbering of 2HA2). Simulations of the protonated AChE show much more stable and less mobile omega loop and Trp86. Such omega loop conformations are not seen in any of the crystal structures of AChE. Furthermore, a great deal of experimental evidence disproves that larger conformational rearrangements of omega loop would take part in the reaction mechanism [2]. (en)
Title	pKa Calculation for Selected Active Site Residues in Acetylcholinesterase pKa Calculation for Selected Active Site Residues in Acetylcholinesterase (en)
skos:prefLabel	pKa Calculation for Selected Active Site Residues in Acetylcholinesterase pKa Calculation for Selected Active Site Residues in Acetylcholinesterase (en)
skos:notation	RIV/00216224:14740/11:00049966!RIV12-MO0-14740___
http://linked.open...avai/riv/aktivita	P S
http://linked.open...avai/riv/aktivity	P(GD301/09/H004), P(LC06030), P(OVMASUN200901), S
http://linked.open...vai/riv/dodaniDat	2012
http://linked.open...aciTvurceVysledku	Wiesner, Jiří Koča, Jaroslav
http://linked.open.../riv/druhVysledku	O - Ostatní výsledky nezařaditelné do žádného z výše uvedených druhů výsledku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Středoevropský technologický institut
http://linked.open...dnocenehoVysledku	220451
http://linked.open...ai/riv/idVysledku	RIV/00216224:14740/11:00049966
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	acetylcholinesterase; pKa; thermodynamic integration; umbrella sampling; charged species transport; electrostatic potetial; glutamic acid (en)
http://linked.open.../riv/klicoveSlovo	acetylcholinesterase glutamic acid pKa charged species transport electrostatic potetial thermodynamic integration umbrella sampling
http://linked.open...ontrolniKodProRIV	[C5E31C0F7B4F]
http://linked.open...in/vavai/riv/obor	CF
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	2 (xsd:int)
http://linked.open...vavai/riv/projekt	Molecular and structural biology of selected antitumor drugs. From mechanistic studies to chemotherapy of tumors Biomolecular centre Research of acetylcholinesterase reactivation by methods of computation chemistry
http://linked.open...UplatneniVysledku	2011
http://linked.open...iv/tvurceVysledku	Koča, Jaroslav Wiesner, Jiří
http://localhost/t...ganizacniJednotka	14740

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