pKa Calculations of Key Ionizable Protein Residues in Acetylcholinesterase
| Authors | |
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| Year of publication | 2010 |
| Type | Article in Proceedings |
| Conference | UF5 - Book of Contributions |
| MU Faculty or unit | |
| Citation | |
| Web | http://indico.cern.ch/conferenceDisplay.py?confId=69338%20[+] |
| Field | Physical chemistry and theoretical chemistry |
| Description | One of the most abundant quantities characterising proteins is its isoelectric point, which is directly dependent on the number of charged ionizable residues, on the pKa of all ionizable residues more exactly. In this work, the pKa of buried protein aminoacids are estimated using method based on molecular dynamics called thermodynamic integration. The main scope is to compute pKa in acetylcholinesterase, but the computations on a small protein, thioredoxin, will be also presented as benchmark calculations. |
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