Quantum and quantum-classical studies of phosphoryl-transfer mechanisms in model systems

• Autorzy: Grochowski P
• Języki publikacji: EN

Słowa kluczowe

EN

gene regulation; metabolism; enzyme; signal transduction; phosphoryl-transfer process; phosphatase; phosphoryl-transfer mechanism; kinase

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2003
• Tom: 08
• Numer: 2A
• Opis fizyczny: p.617-618

Twórcy

autor

Grochowski P

• Warsaw University, Pawinskiego 5A, 02-106 Warsaw, Poland

Bibliografia

• 1. Ho, M.-F., Bramson, N.H., Hansen, E.D., Knowles, R.J. and Kaiser, E.T. Stereochemical course of the phospho group transfer catalyzed by cAMP- dependent protein kinase. J. Am. Chem. Soc. 110 (1988) 2680-2681.
• 2. Błachut-Okrasińska, E., Lesyng, B., Briggs, J.M., McCammon, J.A. and Antosiewicz, J.M. Poisson-Boltzmann model studies of molecular electrostatic properties of the cAMP-dependent protein kinase. Eur. Biophys. J. 28 (1999) 457-467.
• 3. Wojciechowski, M., Grycuk, T., Antosiewicz, J.M. and Lesyng, B. Prediction of secondary ionization of the phosphate group in phosphotyrosine peptides. Biophys. J. 84 (2003) 1-7.
• 4. Ginalski, K., Grochowski, P., Lesyng, B. and Shugar, D. DFT calculations and parameterization of the approximate valence bond method to describe the phosphoryl transfer reaction in a model system. Int. J. Quant. Chem. 90 (2002) 1129-1139.
• 5. Frauenheim, T., Seifert, G., Elstner, M., Hajnal, Z., Jungnickel, G., Porezag, D., Suhai, S. and Scholz, R. A self-consistent charge density-functional based tight-binding method for predictive materials simulations in physics, chemistry and biology. Physica Status Solidi B - Basic Research 217 (2000) 41-62.
• 6. Rakowski, F., Grochowski, P. and Lesyng, B. SCC DFT TB Energy calculations for the phosphoryl-transfer reaction in the PKA active site. Cell. Mol. Biol. Lett. 8 (2003) 603.
• 7. Bala, P., Grochowski, P., Nowinski, K., Lesyng, B. and McCammon, J.A. Quantum-dynamical picture of a multistep enzymatic process: Reaction catalyzed by phospholipase A2. Biophys. J. 79 (2000) 1253-1262.