Paweł Kędzierski, Ph.D.

A3/301A
+48 71 320 3200
Pawel.Kedzierski@pwr.wroc.pl

Publications

  1. B. Ditkowski, N. Holmes, J. Rydzak, M. Donczew, M. Bezulska, K. Ginda, P. Kędzierski, J. ZAkrzewska-Czerwińska, G. Kelemen, D. Jakimowicz, Dynamic interplay of ParA with the polarity protein, Scy, coordinates the growth with chromosome segregation in Streptomyces coelicolor, Open Biology 3 (130006), 1-13 (2013) DOI
  2. K. M. Langner, P. Kędzierski, W. A. Sokalski, J. Leszczynski, Physical nature of ethidium and proflavine interactions with nucleic acid bases in the intercalation plane, J. Phys. Chem. B 110 (19), 9720-9727 (2006) DOI
  3. B. Szefczyk, P. Kędzierski, W. A. Sokalski, J. Leszczynski, Theoretical insights into catalysis by phosphonoacetylaldehyde hydrolase, Mol. Phys. 104 (13-14), 2203-2211 (2006) DOI [copy available upon request]
  4. G. Forde, P. Kędzierski, W. A. Sokalski, A. . E. Forde, G. Hill, J. Leszczynski, Physical nature of interactions within the active site of cytosine-5-methyltransferase, J.Phys.Chem. A 110 (6), 2308-2313 (2006) DOI [Copy available on request]
  5. P. Kędzierski, P. Wielgus, A. Sikora, W. A. Sokalski, J. Leszczynski, Visualization of the Differential Transition State Stabilization within the Active Site Environment, Int. J. Mol. Sci. 5 (4-7), 186-195 (2004) [PDF]
  6. P. Kędzierski, W. A. Sokalski, H. Cheng, J. Mitchell, J. Leszczynski, DFT study of the reaction proceeding in the cytidine deaminase, Chem. Phys. Lett. 381 (5-6), 660-665 (2003) DOI
  7. P. Kędzierski, K. Moreton, A. R. Clarke, J. J. Holbrook, The A245K Mutation Exposes Another Stage of the Bacterial L-Lactate Dehydrogenase Reaction Mechanism, Biochemistry 40 7247-7252 (2001) DOI
  8. P. Kędzierski, W. A. Sokalski, Analysis of Transferability of Atomic Multipoles for Amino Acids in Modeling Macromolecular Charge Distribution from Fragments, J. Comp. Chem. 22 (10), 1082-1097 (2001) DOI
  9. W. A. Sokalski, P. Kędzierski, J. Grembecka, Ab initio study of the physical nature of interactions between enzyme active site fragments in vacuo, Phys. Chem. Chem. Phys. 3 657-663 (2001) DOI
  10. J. Grembecka, P. Kędzierski, W. A. Sokalski, J. Leszczynski, Electrostatic Models of Inhibitory Activity, Int. J. of Quant. Chem. 83 (3-4), 180-192 (2001) DOI
  11. P. Kędzierski, Ph.D. Thesis: Study of the nature of interactions in the active sites of enzymes, (2001) [in Polish]
  12. P. Kędzierski, K. Moreton, A. R. Clarke, J. J. Holbrook, The A245K mutation exposes another stage of the bacterial L-lactate dehydrogenasr reaction mechanism., Biochem. 40 7247-7252 (2001)
  13. P. Kędzierski, W. A. Sokalski, M. Krauss, Nonempirical analysis of nature of catalytic effects in ribonuclease A active site, J. of Comp. Chem. 21 (6), 432-445 (2000) DOI
  14. J. Grembecka, P. Kędzierski, W. A. Sokalski, Nonempirical Analysis of the Nature of the Inhibitor-Active Site Interactions in Leucine Aminopeptidase, Chem. Phys. Lett. 313 (1-2), 385-392 (1999) DOI
  15. W. A. Sokalski, P. Kędzierski, J. Grembecka, P. Dziekoński, K. Strasburger, Theoretical tools for analysis and modelling electrostatic effects in biomolecules, In: Computational Molecular Biology, Vol. 8, Chapter 10, p. 269-396 Editor: Jerzy Leszczyński, Series: Theoretical and Computational Chemistry, Elsevier-Science, New York and Oxford 1999 [ISBN: 0444500308]
  16. P. Kędzierski, M.Sc. Thesis: A comparison of the potential of modelling techniques with results of experiments based on Bacillus stearothermophilus Lactate Dehydrogenase framework, (1995)

Tematy prac dyplomowych i badawczych (Research topics for students)

  1. Racjonalne projektowanie enzymów o zmienionej specyficzności względem substratu.
  2. Teoretyczne badania natury i mechanizmu katalizy enzymatycznej.
  3. Wykorzystanie metod bioinformatyki do przewidywania struktury i funkcji białka na podstawie sekwencji.