People
George A. Kaminski
Associate Professor
Faculty Listing
Office: Life Sciences and Bioengineering Center, 4019
Phone: +1-508-831-4160
Fax: +1-508-831-4116
gkaminski@wpi.edu
Related Information
Educational Background
- B.S./M.S., Moscow Institute of Physics and technology, Moscow, U.S.S.R., 1990
- M.S., Physical Chemistry, Yale University, 1993
- Ph.D., Physical Chemistry, Yale University, 1998
Research & Teaching Interests
Computational physical, biophysical, physical organic chemistry; studying proteins and protein-ligand interactions; developing and applying polarizable force fields
Research
Computer technology has developed dramatically in the past few decades. It is now possible to use it to obtain accurate results of chemical and biochemical interest. However, there is still a great need for the computational chemistry techniques which would fully utilize this potentially available level of accuracy. My research goal is to build a bridge between accurate physical methods and their molecular and biomolecular applications. The primary thrust of my group is in creating and using empirical polarizable force fields for proteins. Describing proteins as molecular systems with constant electrostatic charges on atoms has significant limitations. While it is generally possible to predict protein structure with such techniques, accurate calculation of energetic properties (binding energies, acidity constants, relative conformational energies) often requires many-body effects to be taken into the account. The most common way of doing so is by explicitly introducing electrostatic polarizability, for example, in a form of inducible atomic dipoles. We have demonstrated that correct representation of certain protein-ligand binding energies (especially in the presence of metal ions) is impossible without the explicit use of polarization. We have also been able to reporoduce acidity constants of the carboxyl residues of the OMTKY3 protein within ca. 0.6 pH units by using a polarizable force field. A complete polarizable force field is now being developed to be used for calculating protein pKa's and studying farnesyl transferase inhibition as its first practical applications.
Another research area in my lab is in studying protein and protein-ligand behavior uder mechanical influence. For example, we have recenlty proposed a mechanism which explains induction of apoptosis by low-intensity ultrasound irradiation of cancer cells. This study involved computational investigation of complexes of cross-linked apoptosis inhibitors (XIAP) with the caspase protein and a small molecular antagonist.
Overall, the goal of our research is to bring the combined power of robust physical theory and modern computers into solving chemical and biochemical problems with a high level of accuracy.
Research Grants
- U.S. Army Research Laboratory grant DAAD19-03-2-0012 April 2003 – April 2005 (Co-PI, $152,694). Computer simulations of dendrimers and their complexes.
- National Institutes of Health R01 grant 1 R01 GM074624-01A2, March 2007 – February 2012 (PI, $1,365,000). Protein Simulations with a fast polarizable force field.
Recent Publications
Years of Service at WPI
- Associate Professor, 2008 -