Publications

2018
[121] V. L. Schramm and Schwartz, S. D., “

Promoting vibrations and the function of enzymes. Emerging theoretical and experimental convergence

”, Biochemistry, pp. (in press), 2018. biochem_rev.pdf
[120] X. Chen and Schwartz, S. D., “

Directed evolution as a probe of rate promoting vibrations introduced via mutational change

”, Biochemistry, pp. (in press), 2018. biochem_2018.pdf
[119] C. Luft, Munusamy, E., Pemberton, J., and Schwartz, S. D., “

Molecular dynamics simulation of the oil sequestration properties of a nonionic rhamnolipid

”, J. Phys. Chem. B, vol. 122, pp. 3944-3952, 2018. jpcb_122_3944_2018.pdf jpcb_122_3944_2018_si.pdf
[118] N. Bras, Fernandes, P., Ramos, M., and Schwartz, S. D., “

Mechanistic insights on human phosphoglucomutase revealed by transition path sampling and molecular dynamics calculations

”, Chem. Eur. J, vol. 24, pp. 1978-1987, 2018. chemeurj_24_1978_2018.pdf chemeurj_24_1978_2018_si.pdf
2017
[117] I. Zoi, Antoniou, D., and Schwartz, S. D., “

Electric fields and fast protein dynamics in enzymes

”, J. Phys. Chem. Lett., vol. 8, pp. 6165-6170, 2017. jpcl_8_6165_2017.pdf jpcl_8_6165_2017_si.pdf
[116] R. Eismin, Munusamy, E., Kegel, L., Hogan, D., Schwartz, S. D., and Pemberton, J., “

Evolution of aggregate structure in solutions of anionic monorhamnolipids: experimental and computational results

”, Langmuir, vol. 33, pp. 7412-7424, 2017. langmuir_33_7412_2017.pdf langmuir_33_7412_2017_si.pdf
[115] I. Zoi, Antoniou, D., and Schwartz, S. D., “

Incorporating fast protein dynamics into enzyme design: a proposed mutant aromatic amine dehydrogenase

”, J. Phys. Chem. B, vol. 121, pp. 7290-7298, 2017. jpcb_121_7290_2017.pdf jpcb_121_7290_2017_si.pdf
[114] M. McConnell, Williams, M., Lynn, M., Schwartz, B., Schwartz, S. D., and Tardiff, J., “

Clinically Divergent Mutation Effects on the Structure and Function of the Human Cardiac Tropomyosin Overlap

”, Biochemistry, vol. 56, pp. 3403-3413, 2017. biochem_56_3403_2017.pdf biochem_56_3403_2017_si.pdf
[113] R. Harijan, Zoi, I., Antoniou, D., Schwartz, S. D., and Schramm, V. L., “

Catalytic-site design for inverse heavy-enzyme isotope effects in human PNP

”, Proc. Natl. Acad. Sci. USA, vol. 114, pp. 6456-6461, 2017. pnas_114_6456_2017.pdf pnas_114_6456_2017_si.pdf
[112] E. Munusamy, Luft, C., Pemberton, J., and Schwartz, S. D., “

Structural properties of nonionic monorhamnolipid aggregates in water studied by classical molecular dynamics simulations

”, J. Phys. Chem. B, vol. 121, pp. 5781-5793, 2017. jpcb_121_5781_2017.pdf jpcb_121_5781_2017_si.pdf force_field_parameters.txt
[111] M. Varga, Dzierlenga, M., and Schwartz, S. D., “

Structurally linked dynamics in lactate dehydrogenases of evolutionarily distinct species

”, Biochemistry, vol. 56, pp. 2488-2496, 2017. biochem_56_2488_2017.pdf
2016
[110] X. Pan and Schwartz, S. D., “

Conformational heterogeneity in the Michaelis complex of LDH: an analysis of vibrational spectroscopy using Markov and hidden Markov models

”, J. Phys. Chem. B, vol. 120, pp. 6612-6620, 2016. jpcb_120_6612_2016.pdf jpcb_120_6612_2016_si.pdf
[109] M. Dzierlenga and Schwartz, S. D., “

Targeting a rate-promoting vibration with an allosteric mediator in Lactate Dehydrogenase

”, J. Phys. Chem. Lett., vol. 7, pp. 2591-2596, 2016. jpcl_7_2591_2016.pdf jpcl_7_2591_2016_si.pdf
[108] M. Dzierlenga, Varga, M., and Schwartz, S. D., “

Path sampling methods for enzymatic quantum particle transfer reactions

”, Methods in Enzymology, vol. 577, pp. 21-43, 2016. methenz2016.pdf
[107] M. Varga and Schwartz, S. D., “

Enzymatic kinetic isotope effects from first-principles path sampling calculations

”, J Chem Theory Comput, vol. 12, pp. 2047-2054, 2016. jctc_12_2047_2016.pdf
[106] M. Williams, Lehman, S., Tardiff, J., and Schwartz, S. D., “

Atomic resolution probe for allostery in the regulatory thin filament

”, Proc. Natl. Acad. Sci. USA, vol. 113, pp. 3257-3262, 2016. pnas_113_3257_2016.pdf pnas_113_3257_2016_si.pdf average_structure.pdb_.zip
[105] I. Zoi, Suarez, J., Antoniou, D., Cameron, S., Schramm, V. L., and Schwartz, S. D., “

Modulating enzyme catalysis through mutations designed to alter rapid protein dynamics

”, J. Am. Chem. Soc., vol. 138, pp. 3403-3409, 2016. jacs_138_3403_2016.pdf jacs_138_3403_2016_si.pdf
[104] D. Antoniou and Schwartz, S. D., “

Phase space bottlenecks in enzymatic reactions

”, J. Phys. Chem. B, vol. 120, pp. 433-439, 2016. jpcb_120_433_2016.pdf
[103] Z. Wang, Antoniou, D., Schwartz, S. D., and Schramm, V. L., “

Hydride transfer in DHFR by transition path sampling, kinetic isotope effects, and heavy enzyme studies

”, Biochemistry, vol. 55, pp. 157-166, 2016. biochem_55_157_2016.pdf biochem_55_157_2016_si.pdf
2015
[102] X. Pan and Schwartz, S. D., “

Free Energy Surface of the Michaelis Complex of Lactate Dehydrogenase: A Network Analysis of Microsecond Simulations

”, J. Phys. Chem. B, vol. 119, pp. 5430-5436, 2015. jpcb_119_5430_2015.pdf jpcb_119_5430_2015_si.pdf
[101] M. Dzierlenga, Antoniou, D., and Schwartz, S. D., “

Another Look at the Mechanisms of Hydride Transfer Enzymes with Quantum and Classical Transition Path Sampling

”, J. Phys. Chem. Lett., vol. 6, pp. 1177-1181, 2015. jpcl_6_1177_2015.pdf jpcl_6_1177_2015_si.pdf
[100] I. Zoi, Motley, M., Antoniou, D., Schramm, V. L., and Schwartz, S. D., “

Enzyme homologues have distinct reaction paths through their transition states

”, J. Phys. Chem. B, vol. 119, pp. 3662-3668, 2015. jpcb_119_3662_2015.pdf jpcb_119_3662_2015_si.pdf jpcb_119_3662_2015_1.mpeg jpcb_119_3662_2015_2.mpeg
[99] O. v. der Poorten, Zoi, I., Schwartz, S. D., Cai, M., Hruby, V., and Ballet, S., “

Azepinone-Containing Tetrapeptide Analogues of Melanotropin Lead to Selective hMC4R Agonists and hMC5R Antagonist

”, Medicinal Chemistry Letters, vol. 6, pp. 192-197, 2015. medchemlett_6_192_2015.pdf
[98] J. Masterson and Schwartz, S. D., “

Evolution alters the enzymatic reaction coordinate of dihydrofolate reductase

”, J. Phys. Chem. B, vol. 119, pp. 989-996, 2015. jpcb_119_989_2015.pdf
2014
[97] J. Masterson and Schwartz, S. D., “

The enzymatic reaction catalyzed by lactate dehydrogenase exhibits one dominant reaction path

”, Chem. Phys., vol. 442, pp. 132-136, 2014. chemphys_442_132_2014.pdf

Pages