Abstract
Site directed mutagenesis and computer simulations studies have become valuable tools for the understanding of function-structure relations of proteins. At the current level of computer technology, the quantitative agreement between experimental and molecular simulations results is not always satisfactory for proteins of acetylcholinesterase (AChE) size and complexity. However, the comparison of both types of results can increase dramatically our knowledge on molecular mechanisms of protein action.
presenting author.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Antosiewicz, J., McCammon, J.A., & Gilson, M.K. (1994a) Prediction of pH-dependent properties of proteins, J. Mol. Biol. 238: 415–436.
Antosiewicz, J., Wlodek, S.T., McCammon, J.A., & Gilson M.K. (1994b), Simulation of charge-mutant acetylcholinesterase, Biochemistry, submitted.
Breneman, C.M., & Wiberg, K.B. (1990), Determining atom-centered monopoles from molecular electrostatic potentials. The need for high sampling in formamide conformational analysis, J. Comput.Chem., 11: 361–373.
Clark, T.W., Hanxleden, R.V., McCammon, J.A., & Scott L.R. (1994), Scalable High Performance Computing Conference, Knoxville TN. Available via anonymous ftp from softlib.rice.edu as pub/CRPC-TRs/re-ports/CRPC-TR93356-S.
Frisch, M.J., Trucks, G.W., Head-Gorgon, M., Gill, P.M.W., Wong, M.W., Foresman, J.B., Johnson, B.G., Schlegel, H.B., Robb, M.A., Replogle, E.S., Gomperts, R., Abdres, J.L., Raghavachari, K., Binkley, J.S., Gonzalez, C., Martin, R.L., Fox, D.J., Defrees, D.J., Baker, J., Stewart, J.J.P., & Pople, J.A., (1992), Gaussian 92, Revision E.2.
Gregor, V.E., Emmerling, M.R., Lee, C., & Moore, C.J. (1992), The synthesis and in vitro acetylcholinesterase and butyrylcholinesterase inhibition activity of tacrine (Cognex) derivatives, Bioorg. Med. Chem. Letters, 2: 861–864.
Harel, M., Schalk, I., Ehret-Sabatier, L., Bouet, F., Goeldner, M., Hirth, C., Axelsen, P., Silman, I., & Sussman, J.L. (1993), Quaternary ligand binding to aromatic residues in the active site gorge of acetylcholinesterase. Proc. Natl. Acad. Sci, USA, 90: 9031–9035.
Jorgensen, W.L., & Tirado-Rives J., (1988), The OPLS potential function for proteins: energy minimizations for crystals of cyclic peptides and crambin, J. Am. Chem. Soc. 110: 1657–1666.
Madura, J.D., Davis, M.E., Gilson, M.K., Wade, R.C., Luty, B.A., & McCammon, J.A. (1994), Biological Applications of electrostatic calculations and Brownian dynamics simulations, Rev. Comp. Chem. 5: 229–267.
McCammon, J.A., & Harvey S.C. (1987). Dynamics of Proteins and Nucleic Acids, University Press, Cambridge, 1987.
Quinn, D., Seravalli, J., Nair, H.K., Radic, Z. Vellom, D.C., Pickering, N.A., & Taylor P. (1995), Electrostatic influence on acylation reaction dynamics of acetylcholinesterase-catalyzed hydrolysis, Biochemistry, in press.
Shafferman, A., Ordentlich, A., Barak, D., Kronman, C., Ber, R., Bino, T., Ariel, N., Osman, R., & Velan, B. (1994), Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase, EMBO J., 13: 3445–3448.
Straatsma, T.P., & McCammon, J.A. (1991), Multiconfiguration thermodynamic integration, J. Chem. Phys., 95: 1175–1188.
Susmann, J.L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Token, L., & Silman, I. (1991), Atomic structure of acetylcholinesterase from torpedo californica: Aprototypic acetylcholine-binding protein, Science 233: 872–879.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media New York
About this chapter
Cite this chapter
Wlodek, S.T., Antosiewicz, J., Gilson, M.K., McCammon, J.A., Clark, T.W., Scott, L.R. (1995). Computer Modeling of Acetylcholinesterase and Acetylcholinesterase-Ligand Complexes. In: Quinn, D.M., Balasubramanian, A.S., Doctor, B.P., Taylor, P. (eds) Enzymes of the Cholinesterase Family. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1051-6_21
Download citation
DOI: https://doi.org/10.1007/978-1-4899-1051-6_21
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-1053-0
Online ISBN: 978-1-4899-1051-6
eBook Packages: Springer Book Archive