pKa Calculation for Selected Active Site Residues in Acetylcholinesterase
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F11%3A00049966" target="_blank" >RIV/00216224:14740/11:00049966 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
pKa Calculation for Selected Active Site Residues in Acetylcholinesterase
Original language 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 conformationalchanges 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].
Czech name
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Czech description
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Classification
Type
O - Miscellaneous
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů