Email: dominika.bystranowska@pwr.edu.pl

Unit: Faculty of Chemistry » Department of Biochemistry, Molecular Biology and Biotechnology

Gdańska 7/9, 50-344 Wrocław
building F-4, room C-18
phone +48 71 320 6334

ORCID: 0000-0002-6745-5355

Office hours

• Monday 11:00 am - 1:00 pm; Thursday 9:00 am - 11:00 am

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Research fields

• Biochemical and structural characterization of proteins of potential physiological importance with a special emphasis on intrinsically disordered proteins; the effect of environmental factors on protein conformation changes; protein-ligand, protein-protein and protein-nucleic acid interactions; single molecule fluorescence biophysics (smFRET and FCS), circular dichroism (CD) spectroscopy, analytical ultracentrifugation (AUC).

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Recent papers

2024

• Lenda R., Zhukova L., Ożyhar A., Bystranowska D. Deciphering the dual nature of nesfatin-1: a tale of zinc ion's Janus-faced influence, (2024) Cell Communication and Signaling, 22(1), 298. DOI: 10.1186/s12964-024-01675-x

2023

• Skorupska-Stasiak A., Bystranowska D., Tran J.B., Krężel A., Ożyhar A. Nesfatin-3 possesses divalent metal ion binding properties, which remain hidden in the nucleobindin-2 precursor protein (2023) Cell Commun. Signal. 21(1):165. DOI: 10.1186/s12964-023-01181-6
  
• Sołtys K., Tarczewska A., Bystranowska D., Modulation of biomolecular phase behavior by metal ions (2023) Biochim. Biophy. Acta Mol. Cell Res. 1870(8):119567. DOI: 10.1016/j.bbamcr.2023.119567
• Szefczyk M., Szulc N., Gąsior-Głogowska M., Bystranowska D., Żak A., Sikora A., Polańska O., Ożyhar A., Berlicki Ł., The application of the hierarchical approach for the construction of foldameric peptide self-assembled nanostructures (2023) Soft Matter. 19(21):3828-3840. DOI: 10.1039/d3sm00005b

2022

• Lenda R., Padjasek M., Krężel A., Ożyhar A., Bystranowska D., Does one plus one always equal two? Structural differences between nesfatin-1, -2, and nesfatin-1/2 (2022) Cell Commun. Signal., 20(1):163. DOI: 10.1186/s12964-022-00980-7
• Wieczorek E., Wygralak Z., Kędracka-Krok S., Bezara P., Bystranowska D., Dobryszycki P., Ożyhar A., Deep blue autofluorescence reflects the oxidation state of human transthyretin (2022) Redox Biology 56, pp. 102434. DOI: 10.1016/j.redox.2022.102434
• Sołtys K., Tarczewska A., Bystranowska D., Sozańska N., Getting Closer to Decrypting the Phase Transitions of Bacterial Biomolecules (2022) Biomolecules, 12 (7) 907. DOI: 10.3390/biom12070907

2021

• Bystranowska D., Skorupska A., Sołtys K., Padjasek M., Krężel A., Żak A., Kaus-Drobek M., Taube M., Kozak M., Ożyhar A., Nucleobindin-2 consists of two structural components: the Zn²⁺-sensitive N-terminal half, consisting of nesfatin-1 and -2, and the Ca²⁺-sensitive C-terminal half, consisting of nesfatin-3 (2021) Comput. Struct. Biotechnol. J. 19, pp. 4300-4318. DOI: doi.org/10.1016/j.csbj.2021.07.036
• Skorupska A., Lenda R., Ożyhar A., Bystranowska D., The Multifaceted Nature of Nucleobindin-2 in Carcinogenesis (2021) Int J Mol Sci. 22 (11) 5687. DOI: doi.org/10.3390/ijms22115687

• Wieczorek E., Kędracka-Krok S., Bystranowska D., Ptak M., Wiak K., Wygralak Z., Jankowska U., Ożyhar A.,Destabilisation of the structure of transthyretin is driven by Ca² (2021) Int J Biol Macromol. 166, pp. 409-423. DOI: 10.1016/j.ijbiomac.2020.10.199

2020

• Kolonko M., Bystranowska D., Taube M., Kozak M., Bostock M., Popowicz G., Ożyhar A., Greb-Markiewicz B., The intrinsically disordered region of GCE protein adopts a more fixed structure by interacting with the LBD of the nuclear receptor FTZ-F1 (2020) Cell Commun Signal. 18(1):180. DOI: 10.1186/s12964-020-00662-2.

• Skorupska A., Bystranowska D., Dąbrowska K., Ożyhar A., Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein (2020) International Journal of Biological Macromolecules, 154, pp. 1091-1104. DOI: doi.org/10.1016/j.ijbiomac.2020.03.110

2018

• Chinnaraj M., Chen Z., Pelc L.A., Grese Z., Bystranowska D., Di Cera E., Pozzi N., Structure of prothrombin in the closed form reveals new details on the mechanism of activation (2018) Scientific Reports, 8, art. no. 2945. DOI: 10.1038/s41598-018-21304-1

2017

• Kozłowska M., Tarczewska A., Jakób M., Bystranowska D., Taube M., Kozak M., Czarnocki-Cieciura M., Dziembowski A., Orłowski M., Tkocz K., Ożyhar A., Nucleoplasmin-like domain of FKBP39 from Drosophila melanogaster forms a tetramer with partly disordered tentacle-like C-terminal segments (2017) Scientific Reports, 7, art. no. 40405. DOI: 10.1038/srep40405

2016

• Pozzi N., Bystranowska D., Zuo X., Di Cera E., Structural architecture of prothrombin in solution revealed by single molecule spectroscopy (2016) Journal of Biological Chemistry, 291 (35), pp. 18107-18116. DOI: 10.1074/jbc.M116.738310

 

Papers in DONA database