Daniel Konstantinovsky
Prediction of nonlinear spectra of biomolecules, biological PCET
daniel.konstantinovsky@yale.
B.S. in Chemistry, 2016
Haverford College, Haverford, PA
Location
Contact
Sharon Hammes-Schiffer
Sterling Professor of Chemistry
Sterling Chemistry Lab, Rm 178
Department of Chemistry
Yale University
225 Prospect Street, PO Box 208107
New Haven, CT 06520-8107
Phone: (203) 436-3936
e-mail: sharon.hammes-schiffer@yale.edu
Tags in Publications
[FeFe]-hydrogenase models [NiFe]-hydrogenase models BLUF catalysis coupled motions Density functional theory treatment Dihydrofolate reductase DNA DNA polymerase electron transfer Electron-proton correlation electrostatics enzyme catalysis Escherichia coli Hartree-Fock HDV ribozyme hydride transfer hydrogen atom transfer hydrogen bonding hydrogen evolution hydrogen tunneling inverted region behavior Ketosteroid Isomerase kinetic isotope effect Liver alcohol dehydrogenase metal ion molecular dynamics molecular electrocatalysts multicomponent density functional theory Nonadiabatic dynamics nonadiabaticity Nuclear quantum effects nuclear-electronic orbital photoinduced proton-coupled electron transfer proton relays Proton transfer proton-coupled electron transfer QM/MM real-time nuclear-electronic orbital reorganization energies ribozyme solvent dynamics Soybean lipoxygenase Surface hopping Vibrational analysis
Design of an electrostatic frequency map for the NH stretch of the protein backbone and application to chiral sum frequency generation spectroscopy
345. D. Konstantinovsky, E. A. Perets, T. Santiago, K. Olesen, Z. Wang, A. V. Soudackov, E. C. Y. Yan, S. Hammes-Schiffer, “Design of an electrostatic frequency map for the NH stretch of the protein backbone and application to chiral sum frequency generation spectroscopy,” J. Phys. Chem. B (in press). DOI: 10.1021/acs.jpcb.3c00217
Detecting first hydration shell structure around biomolecules at interfaces
335. D. Konstantinovsky, E. A. Perets, T. Santiago, L. Velarde, S. Hammes-Schiffer, and E. C. Y. Yan, “Detecting first hydration shell structure around biomolecules at interfaces,” ACS Cent. Sci. 8, 1404-1414 (2022). DOI: 10.1021/acscentsci.2c00702
Kinetic model for reversible radical transfer in ribonucleotide reductase
330. C. R. Reinhardt, D. Konstantinovsky, A. V. Soudackov, and S. Hammes-Schiffer, “Kinetic model for reversible radical transfer in ribonucleotide reductase,” Proc. Nat. Acad. Sci. USA 119, e2202022119 (2022). DOI: 10.1073/pnas.2202022119