Theoretical Studies In Biophysics and Biochemistry
The research in my group has three broad aims. First we wish to develop approximate methods that allow the practical prediction of the dynamics of chemical reactions in biomolecular systems. Because even in large biological systems, many events are governed by quantum mechanics, we seek to develop methods that allow the study quantum proces ses in complex systems. In biological systems, some enzymatic reactions, which involve the transfer of a hydrogen atom, seem to proceed almost entirely by quantum mechanical tunneling. Our research has focused on the use of Feynman Path Integrals to study these complex systems.
The second aim of my work is to understand the atomic level processes by which enzymes accomplish their extraordinary specific catalytic effect. We employ such methods as Transition Path Sampling and analysis of the stochastic separatrix to develop detailed pictures of enzymatic mechanism. Using such approaches we have uncovered the extraordinary possibility that in certain enzyme systems, evolution has developed the protein body of the enzyme to channel thermal energy to the active site to promote reaction. This concept of directed protein motions, which we have termed promoting vibrations, is now an area of international research focus.
The third aim of my research is to develop and apply new methods to the study of protein complexes that make up the machinery of cells. In particular, with Jil Tardiff's group, we are interested in understanding both wildtype and mutant functions of the cardiac thin filament in regulating the sarcomere, and in particular how mutations cause disease.
P.J. Guinto, E.P. Manning,∗ S.D. Schwartz, and J.C. Tardiff Computational Characterization of Mutations in Cardiac Troponin T Known to Cause Familial Hypertrophic Cardiomyopathy, J.T.C.C. 6, 413-419 (2007)
D. Antoniou, D. Gelman, and S.D. Schwartz A new mixed quantum/semiclassical propagation method, J. Chem. Phys., 126, 184107 (2007)
J.R.E.T. Pineda, R. Callender, and S.D. Schwartz Ligand binding and protein dynamics in lactate dehydrogenase, Biophysical Journal, 93, 1474-1483 (2007)
S. Quaytman and S.D. Schwartz The reaction coordinate of an enzymatic reaction: TPS studies of lactate dehydrogenase, P.N.A.S. USA, 104, 12253-12258 (2007)
S. Saen-Oon, M. Ghanem, V.L. Schramm, and S.D. Schwartz Remote mutations and active site dynamics correlate with catalytic properties of purine nucleoside phosphorylase, Biophysical Journal 94, 4078-4088 (2008)
M. Ghanem, S. Saen-oon, N. Zhadin, C. Wing, S.M. Cahill, S.D. Schwartz, R.Callender, and V.L. Schramm Tryptophan-free Human PNP Reveals Catalytic Site Interactions, Biochemistry, 47, 3202-3215 (2008)
Gelman and S.D. Schwartz Tunneling Dynamics with a mixed quantum classical method. Quantum corrected propagator with frozen Gaussian wavepackets, J. Chem. Phys., 129, 024504 (2008)
S. Saen-Oon, V.L. Schramm, and S.D. Schwartz Transition path sampling study of the Reaction Catalyzed by Purine Nucleoside Phosphorylase, Z. Phys. Chem., 222, 1359-1374 (2008)
S. Saen-Oon, S. Quaytman, V.L. Schramm, and S.D. Schwartz Atomic Detail of Chemical Transformation at the transition state of an enzymatic reaction, P.N.A.S., 105, 16543-16548 (2008)
D. Gelman and S.D. Schwartz Modeling vibrational resonance in linear hydrocarbon chain with a mixed quantum-classical method, Journal of Chemical Physics, 130 134110 (2009)
S. Quaytman and S.D. Schwartz Comparison Studies of the Human Heart and Bacillus stearothermophilus Lactate Dehydrogenase by Transition Path Sampling, J. Phys. Chem. A, 113, 1892-1897 (2009)
D. Antonio and S.D. Schwartz The stochastic separatrix and the reaction coordinate for complex systems, Journal of Chemical Physics, 130 151103 (2009)
S.D. Schwartz and V.L. Schramm Enzymatic catalysis and the nature of transition state barrier crossing, Nature Chemical Biology, 5, 551-558 (2009)
D. Antoniou and S.D. Schwartz Approximate inclusion of quantum effects in Transition Path Sampling, J. Chem. Phys., 131, 224111 (2009)
D. Gelman and S.D. Schwartz Dissipative dynamics with the corrected propagator method. Numerical comparison between fully quantum and mixed quantum/classical simulations., Chemical Physics 370, 62-69 (2010) (Eli Pollak Festschrift)
S. Quaytman-Machleder, J.R.E.T. Pineda, and S.D. Schwartz On the Origin of the Chemical Barrier and Tunneling in Enzymes, Journal of Physical Organic Chemistry, 23, 690-695 (2010)
J.R.E.T Pineda, D. Antoniou, and S.D. Schwartz Slow conformational motions that favor sub-ps motions important for catalysis, J. Phys. Chem. B114, 15985-15990 (2010)
D. Gelman and S.D. Schwartz Finite temperature application of the corrected propagator method to reactive dynamics in a condensed phase environment, J. Chem. Phys., 134, 034109 (2011)
More Information About Dr. Steven Schwartz
Material in this section is provided by individual faculty members who are solely responsible for its accuracy and content.
Albert Einstein College of Medicine
Jack and Pearl Resnick Campus
1300 Morris Park Avenue
Ullmann Building, Room 213
Bronx, NY 10461