About: Calculating pKa of selected active site aminoacids in acetylcholinesterase

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Acetylcholinesterase (AChE) is an important enzyme participating in nerve signal transmission connected with Alzheimer disease and nerve agent poisoning. Initial molecular dynamics simulations using the Amber force field 03 have revealed a strong dependence of the dynamics on the protonation state of the AChE's active site. Simulations of the protonated AChE were much more stable than that of the deprotonated form where significant changes in the vicinity of the charged residues occurred. AChE's active site contains three glutamic acid residues located close to each other (less than 8 A in the crystal structure). Using thermodynamic integration and the Amber force field 99SB, the pKa of these three glutamic acid residues was calculated. The calculated pKa shift values appear to be overestimated and differ for forward and backward runs significantly. According to the results, AChE should have two of the three glutamate residues protonated. Acetylcholinesterase (AChE) is an important enzyme participating in nerve signal transmission connected with Alzheimer disease and nerve agent poisoning. Initial molecular dynamics simulations using the Amber force field 03 have revealed a strong dependence of the dynamics on the protonation state of the AChE's active site. Simulations of the protonated AChE were much more stable than that of the deprotonated form where significant changes in the vicinity of the charged residues occurred. AChE's active site contains three glutamic acid residues located close to each other (less than 8 A in the crystal structure). Using thermodynamic integration and the Amber force field 99SB, the pKa of these three glutamic acid residues was calculated. The calculated pKa shift values appear to be overestimated and differ for forward and backward runs significantly. According to the results, AChE should have two of the three glutamate residues protonated. (en)
Title	Calculating pKa of selected active site aminoacids in acetylcholinesterase Calculating pKa of selected active site aminoacids in acetylcholinesterase (en)
skos:prefLabel	Calculating pKa of selected active site aminoacids in acetylcholinesterase Calculating pKa of selected active site aminoacids in acetylcholinesterase (en)
skos:notation	RIV/00216224:14740/11:00049967!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	189012
http://linked.open...ai/riv/idVysledku	RIV/00216224:14740/11:00049967
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	acetylcholinesterase; thermodynamics integration; pKa; glutamic acid (en)
http://linked.open.../riv/klicoveSlovo	acetylcholinesterase glutamic acid pKa thermodynamics integration
http://linked.open...ontrolniKodProRIV	[7D8D0D014F4D]
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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