Assistant Professor of Chemistry
Education
B.S./M.S. Applied Mathematics and Physics, Moscow
Institute of Physics and technology (1990)
Ph.D. Chemistry, Yale University (1998)
Contact Information
250 Dow Science, Department of Chemistry
Phone: (989) 774-3441 Fax: (989)-774-3883
e-mail: kamin1ga @ cmich.edu
http://www.cst.cmich.edu/units/chm/people/G_Kaminski.htm
Research Fields
Computational chemistry, modeling protein-ligand interactions,
calculating protein acidity constants (pKa shifts), creating polarizable
force fields.
Current Research Projects
Many biologically and pharmaceutically relevant applications depend on
our ability to quantitatively describe interactions between proteins of
between a protein and another molecule. For example, conditions ranging
from common cold to cancer can be treated or controlled by inhibiting
certain key protein molecules. Therefore, building such inhibitors is an
important target for pharmaceutical industry. Since explicit
experimental synthesis of all potential drug candidates can be a long a
expensive process, it is very advantageous to simulate complexes of
potential drugs with proteins by computational means. Unfortunately, the
accuracy of these simulations are often not quite as high as would be
desired. My work is aimed at contributing to solving this problem by
explicitly treating electrostatic polarization of protein and ligand
molecules. A fast second-order polarization approach is used to make
sure that the computational cost of these simulations is not
prohibitively high. One of the main applied target is currently
inhibition of farnesyl transferase. This project is funded by the
National Institutes of health.
Selected Publications
“Electrostatic
Polarization Is Crucial for Reproducing pKa Shifts of Carboxylic
Residues In Turkey Ovomucoid Third Domain”, MacDermaid, C. M.; Kaminski,
G. A., J. Phys. Chem. B, 111, 9036-9044, 2007.
“Accurate Prediction of
Absolute Acidity Constants in Water with a Polarizable Force Field:
Substituted Phenols, Methanol, and Imidazole”, Kaminski G.A., J.
Phys. Chem. B,
109,
5884-5890, 2005.
“Pseudospectral Local
Second-Order Moller-Plesset Methods for Computation of Hydrogen Bonding
Energies for Molecular Pairs”, Kaminski, G.A.; Maple, J.R.; Murphy, R.B.;
Braden, D. Friesner, R.A., J. Chem. Theory Comput., 1,
248-254, 2005.
“A Polarizable Force
Field Methodology for Gas Phase and Continuum Solvent Computations of
Protein Binding with Medicinal Ligands”, Maple, J.R.; Cao, Y.X.; Damm,
W.; Halgren, T.A.; Kaminski, G.A.; Zhang, L.Y.; Friesner, R.A. J.
Chem. Theory Comput., 1, 694-715, 2005.
“Development of an Accurate and Robust Polarizable Molecular Mechanics
Force Field from An Initio Quantum Chemistry”, Kaminski, G.A.;
Stern, H.A.; Berne, B.J.; Friesner, R.A., J. Phys. Chem. A,
108, 621-627, 2004.
“A Computationally
Inexpensive Modification of the Point Dipole Electrostatic Polarization
Model for Molecular Simulations”, Kaminski, G.A.; Zhou, R.; Friesner,
R.A., J. Comp. Chem., 24, 267-276, 2003.
Figure below: A fragment of the OMTKY3
protein used in protein pKa shifts study with a polarizable force field.
Used in
the project described in: J. Phys. Chem. B, 111,
9036-9044, 2007.