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Warsaw University Faculty of Physics
WERSJA POLSKA  Research    People    Education
Name: Dr.Beata Wielgus-Kutrowska
Address: Department of Biophysics, Institute of Experimental Physics, Warsaw University, Żwirki i Wigury 93, 02-089 Warsaw, Poland
Phone: +48 22 5540789
E-mail: beata@biogeo.uw.edu.pl

Research interests:
I. Understanding of the mechanism of enzymatic catalysis of phosphorolysis reaction by enzyme - purine nucleoside phosphorylase (PNP) on the base of the crystallographic structure of this protein and its behavior in solution measured spectroscopically.
II. Protein folding and aggregation.
Close cooperation with Agnieszka Bzowska. and Patricia Clark, University of Notre Dame, USA.

Professional experience:
1993 Msc. in physics and biophysics, Faculty of Physics, Warsaw University, Warsaw, Poland.
1993-1999 Ph.D. Research, Department of Biophysics, Institute of Experimental Physics, Warsaw University, Warsaw, Poland.
1999 PhD in physics and biophysics, Department of Biophysics, Institute of Experimental Physics, Warsaw University, Warsaw, Poland.
2000 - Adjunct, Department of Biophysics, Institute of Experimental Physics, Warsaw University, Warsaw, Poland.
1996-2001 Practical research as a Visiting Scientist in the laboratory of Prof. Wolfram Saenger, at Institute of Crystallography, Freie Universität, Berlin.
2003 Postdoctoral training at Dr. Patricia Clark laboratory, University of Notre Dame, Notre Dame, Indiana, USA.
Selected publications 1996-2005:
  1. J. Antosiewicz, K Breer, A. Bzowska, B. Wielgus-Kutrowska, On the analysis of fluorimetric titration curves of purine nucleoside phosphorylase. Nucleic Acids Symp Ser (Oxf) 52, 671-672 (2008).
  2. K. Breer, B. Wielgus-Kutrowska, M. Hashimoto, S. Hikishima, T. Yokomatsu, R.H. Szczepanowski, M. Bochtler, A. Girstun, K. Staron, A. Bzowska, Thermodynamic studies of interactions of calf spleen PNP with acyclic phosphonate inhibitors. Nucleic Acids Symp Ser (Oxf) 52, 663-664 (2008).
  3. K Breer, A. Girstun, B. Wielgus-Kutrowska, K. Staroń, A. Bzowska, Overexpression, purification and characterization of functional calf purine nucleoside phosphorylase (PNP). Protein Expr Purif. 61, 122-130 (2008).
  4. K Stepniak, A. Girstun, B. Wielgus-Kutrowska, K. Staroń, A. Bzowska, Cloning, expression, purification, and some properties of calf purine nucleoside phosphorylase. Nucleosides Nucleotides Nucleic Acids 6-7, 855-859 (2007).
  5. J.M. Antosiewicz, B. Wielgus-Kutrowska, M. Długosz, A. Holy, A. Bzowska, Kinetics of binding of multisubstrate analogue inhibitor (2-amino-9-[2-(phosphonomethoxy)ethyl]-6-sulfanylpurine) with trimeric purine nucleoside phosphorylase. Nucleosides Nucleotides Nucleic Acids 8-9, 969-974 (2007).
  6. B. Wielgus-Kutrowska, M. Narczyk. A. Buszko, A. Bzowska, P. Clark, Folding and unfolding of non-fluorescent mutant of green fluorescent protein. J. Phys.: Condens. Matter 19, 285223 (2007).
  7. B. Wielgus-Kutrowska, J. Antosiewicz, M. Długosz, A. Holý, A. Bzowska, Towards the mechanism of trimeric purine nucleoside phosphorylases: stopped-flow studies of binding of multisubstrate analogue inhibitor - 2-amino-9-[2-(phosphonomethoxy)-ethyl]-6-sulfanylpurine. Biophys. Chem. 125, 260-268 (2007).
  8. B. Wielgus-Kutrowska, A. Bzowska, Probing the mechanism of purine nucleoside phosphorylase by steady-state kinetic studies and ligand binding characterization determined by fluorimetric titrations. Biochim. Biophys. Acta 1764, 887-902 (2006).
  9. B. Wielgus-Kutrowska, A. Bzowska, Kinetic properties of Cellulomonas sp. purine nucleoside phosphorylase with typical and non-typical substrates: implications for the reaction mechanism. Nucleosides, Nucleotides and Nucleic Acids 5-7, 471-476 (2005).
  10. A. Bzowska, K. Stepniak, M. Olasek, M. Długosz, B. Wielgus-Kutrowska, J. Antosiewicz, A. Holy, G. Koellner, A. Stroh, G. Raszewski, T. Steiner and J. Frank, Attemps to differentiate subunits of trimeric and hexameric purine nucleoside phosphorylase by crystal structure and solution studies using purine bases, modified purine nucleosides, acyclonucleosides and their phoshonate analogues. Chemistry of Nucleic Acid Components, Collection Symposium Series, vol. 7, 133-142 (2005).
  11. A. Bzowska, G. Koellner, B. Wielgus-Kutrowska, A. Stroh, G. Raszewski, A. Holý, T. Steiner, J. Frank, Crystal structure of calf spleen purine nucleoside phosphorylase with two full trimers in the asymmetric unit: important implications for the mechanism of catalysis. J. Mol. Biol. 342, 1015-1032 (2004).
  12. B. Wielgus-Kutrowska, A. Holy, J. Frank, G. Koellner and A. Bzowska, Interactions of trimeric purine nucleoside phosphorylases with ground state analogues - calorimetric and fluorimetric studies. Nucleosides, Nucleotides and Nucleic Acids 22, 1695-1698 (2003).
  13. B. Wielgus-Kutrowska, A. Bzowska, J. Tebbe, G. Koellner and D. Shugar, Purine nucleoside phosphorylase from Cellulomonas sp.: physicochemical properties and binding of substrates determined by ligand-dependent enhancement of enzyme intrinsic fluorescence, and by protective effects of ligands on thermal inactivation of the enzyme. Biochim. Biophys. Acta 1597, 320-334 (2002).
  14. G. Koellner, A. Bzowska, B. Wielgus-Kutrowska, M. Luić, T. Steiner, W. Saenger and J. Stępiński, Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism. J. Mol. Biol. 315, 351-371 (2002).
  15. B. Wielgus-Kutrowska, J. Tebbe, J. Wierzchowski, D. Shugar, W. Saenger, G. Koellner and A. Bzowska, Binding of substrates by purine nucleoside phosphorylase (PNP) from Cellulomonas sp. - kinetic and spectrofluorimetric studies. Nucleosides and Nucleotides 18, 871-872 (1999).
  16. J. Tebbe, A. Bzowska, B. Wielgus-Kutrowska, W. Schröder, Z. Kazimierczuk, D. Shugar, W. Saenger, W. and G. Koellner, Crystal structures of purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implications of the molecular mechanism of trimeric PNPs. J. Mol. Biol. 294, 1239-1255 (1999).
  17. A. Bzowska, L. Magnowska, B. Wielgus-Kutrowska and Z. Kazimierczuk, Synthesis of 2-chloro-6-aryloxy- and 2-chloro-6-alkoxyarylpurines and their properties in purine nucleoside phosphorylase (PNP) system. Nucleos. And Nucleot.18 (4-5), 873-874 (1999).
  18. B. Wielgus-Kutrowska, J. Tebbe, W. Schröder, M. Luič, D. Shugar, W. Saenger, G. Koellener and A. Bzowska, Cellulomonas sp. Purine Nucleoside Phosphorylase (PNP): Comparison with Human and E. Coli Enzymes. Adv. Exp. Med. Biol. 431, 259-264, Plenum Publishing Corp., New York (1998) .
  19. A. Bzowska, J. Tebbe, M. Luič, B. Wielgus-Kutrowska, W. Schröder, D. Shugar, W. Saenger, and G. Koellener, Crystallization and preliminary studies of purine nucleoside phosphorylase from Cellulomonas sp. Acta Cryst. D54, 1061-1063 (1998).
  20. B. Wielgus-Kutrowska, E. Kulikowska, J. Wierzchowski,A. Bzowska and D. Shugar, Nicotinamide riboside - an unusual, non-typical substrate of purified purine nucleoside phosphorylases. Eur. J. Biochem. 243, 408-414 (1997).
  21. J. Wierzchowski, B. Wielgus-Kutrowska and D. Shugar, Fluorescence emission of 8-azapurines and their nucleosides, and application to the kinetic reverse synthetic reaction of purine nucleoside phosphorylase. Biochim. Biophys. Acta 1290, 9-17 (1996).
  22. J. Tebbe, B. Wielgus-Kutrowska, W. Schröder, M. Luič, D. Shugar, W. Saenger, G. Koellener and A. Bzowska, Purine nucleoside phosphorylase (PNP) from Cellulomonas sp., a third class of PNP different from both "low-molecular weight" mammalian and "high-molecular weight" bacterial PNPs. Miami, Nature Biotechnology, Short Reports, Vol. 8, p. 90, Oxford University Press (1996).
Participation in research projects:
  1. Biophysical bases of purine nucleoside phosphorylase mechanism, and synthesis and biological evaluation of inhibitors - potential drugs
  2. De novo folding of Green Fluorescent Protein in the aspect of applications in biotechnology and molecular biology