About: Alternative entrances into the acetylcholinesterase active site

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Alternative entrances into the acetylcholinesterase active site 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)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Back door to the active site of acetylcholinesterase (AChE) and its involvement in the catalytic cycle of this enzyme are a really controversial subject. The back door could explain the contrast of a very high AChE catalytic efficiency and the narrow and long access to the active site located in the middle of the protein. Back door could facilitate the diffusion of reaction products - choline or acetic acid after the cleavage of acetylcholine. Back door was seen only in a molecular dynamics of AChE, but for a very short times and its existence was not confirmed experimentally. Herein we present a molecular dynamics of AChE, where the back door opening appears on a nanosecond time scale. We also present a molecular dynamics of AChE, where the back door do not open at all, or where large conformational changes of AChE omega loop occur instead of back door opening events. Back door to the active site of acetylcholinesterase (AChE) and its involvement in the catalytic cycle of this enzyme are a really controversial subject. The back door could explain the contrast of a very high AChE catalytic efficiency and the narrow and long access to the active site located in the middle of the protein. Back door could facilitate the diffusion of reaction products - choline or acetic acid after the cleavage of acetylcholine. Back door was seen only in a molecular dynamics of AChE, but for a very short times and its existence was not confirmed experimentally. Herein we present a molecular dynamics of AChE, where the back door opening appears on a nanosecond time scale. We also present a molecular dynamics of AChE, where the back door do not open at all, or where large conformational changes of AChE omega loop occur instead of back door opening events. (en)
Title	Alternative entrances into the acetylcholinesterase active site Alternative entrances into the acetylcholinesterase active site (en)
skos:prefLabel	Alternative entrances into the acetylcholinesterase active site Alternative entrances into the acetylcholinesterase active site (en)
skos:notation	RIV/00216224:14310/07:00020234!RIV11-GA0-14310___
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GD204/03/H016), P(LC06030), Z(MSM0021622413)
http://linked.open...vai/riv/dodaniDat	2011
http://linked.open...aciTvurceVysledku	Wiesner, Jiří Koča, Jaroslav Kříž, Zdeněk
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 / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	409130
http://linked.open...ai/riv/idVysledku	RIV/00216224:14310/07:00020234
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	computational chemistry; computer modeling; molecular dynamics; MD; acetycholinesterase; AChE; alternative entrances; back door; side door; Trp86; Trp84 (en)
http://linked.open.../riv/klicoveSlovo	AChE MD computational chemistry molecular dynamics computer modeling acetycholinesterase Trp84 Trp86 alternative entrances back door side door
http://linked.open...ontrolniKodProRIV	[E696EA7BF1F0]
http://linked.open...in/vavai/riv/obor	CF
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	3 (xsd:int)
http://linked.open...vavai/riv/projekt	Biomolecular centre Structural biophysics of macromolecules
http://linked.open...UplatneniVysledku	2007
http://linked.open...iv/tvurceVysledku	Koča, Jaroslav Wiesner, Jiří Kříž, Zdeněk
http://linked.open...n/vavai/riv/zamer	Proteiny v metabolismu a při interakci organismů s prostředím
http://localhost/t...ganizacniJednotka	14310

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 48 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software