YOUR BROWSER IS OUT-OF-DATE.
We have detected that you are using an outdated browser. Our service may not work properly for you. We recommend upgrading or switching to another browser.
Prof. Tadeusz Andruniów, DSc, PhD
Email: tadeusz.andruniow@pwr.edu.pl
Position: Head of Department
Unit: Faculty of Chemistry » Department of Advanced Materials
ul. M. Smoluchowskiego 23, 50-372 Wrocław
building A-3, room 230
phone +48 71 320 2137
Research fields
- Photoisomerization process in rhodopsin; spectroscopy of fluorescent proteins; resonance Raman spectroscopy of biological systems; high-precision quantum mechanical calculations of spectroscopic properties of biological chromophores; photolysis in cobalamins.
Recent papers
2015
- Tuna D., Lefrancois D., Wolański Ł., Gozem S., Schapiro I., Andruniów T., Dreuw A., Olivucci M., Assessment of approximate coupled-cluster and algebraic-diagrammatic-construction methods for ground- and excited-state reaction paths and the conical-intersection seam of a retinal-chromophore model. Journal of Chemical Theory and Computation. 2015, vol. 11, nr 12, s. 5758-5781.
2013
- Bernini C., Andruniów T., Olivucci M., Pogni R., Basosi R., Sinicropi A., Effects of the protein environment on the spectral properties of tryptophan radicals in Pseudomonas aeruginosa azurin. Journal of the American Chemical Society. 2013, vol. 135, nr 12, s. 4822-4833.
2007
- Frutos L.M., Andruniów T., Santoro F., Ferre N., Olivucci M., Tracking the excited-state time evolution of the visual pigment with multiconfigurational quantum chemistry. Proceedings of the National Academy of Sciences of the United States of America. 2007, vol. 104, nr 19, s. 7764-7769.
2005
- Sinicropi A., Andruniów T., Basosi R., Olivucci M., Properties of the emitting state of the green fluorescent protein resolved at the CASPT2//CASSCF/CHARMM level. Journal of the American Chemical Society. 2005, vol. 127, nr 33, s. 11534-11535.
2004
- Andruniów T., Ferre N., Olivucci M., Structure, initial excited-state relaxation, and energy storage of rhodopsin resolved at the multiconfigurational perturbation theory level. Proceedings of the National Academy of Sciences of the United States of America. 2004, vol. 101, nr 52, s. 17908-17913.
