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Department of Physical Biochemistry



Prof. dr hab. Marta Dziedzicka–Wasylewska
room: C021 (2.01.22), phone: +48 12 664 61 22, e-mail:


Dr hab. Sylwia Kędracka-Krok
room: C020 (2.01.21), phone: +48 12 664 61 48, e-mail:

Dr hab. Andrzej Górecki
room: C023 (2.01.24), phone: +48 12 664 61 51, e-mail:

Dr hab. Sylwia Łukasiewicz
room: C022 (2.01.23), phone: +48 12 664 61 34, e-mail:

Dr. Piotr Bonarek
room: C023 (2.01.24), phone: +48 12 664 61 51, e-mail:

Dr. Agnieszka Polit
room: C019 (2.01.20), phone: +48 12 664 61 56, e-mail:

Dr. Ewa Błasiak
room: C019 (2.01.20), phone: +48 12 664 61 56, e-mail:

Dr. Ewelina Fic
room: C022 (2.01.23), phone: +48 12 664 61 34, e-mail:

Dr. Małgorzata Figiel
room: C022 (2.01.23), phone: +48 12 664 61 34, e-mail:

Dr. Paweł Mystek
room: C024 (2.01.25), phone: +48 12 664 61 54, e-mail:

Dr. Jakub Nowak
room: C025 (2.01.26), phone: +48 12 664 61 55 e-mail:

Mgr Klaudia Drzymała 
room: C025 (2.01.26), phone: +48 12 664 61 55 e-mail:


PhD students

Mgr Beata Rysiewicz, room: C024 (2.01.25), phone: +48 12 664 61 54
Mgr Julia Łakomska, room: C025 (2.01.26), phone: + 48 12 664 61 55
Mgr Dorota Mularczyk, room: C025 (2.01.26), phone: + 48 12 664 61 55
Mgr Agata Kowalik, room: C025 (2.01.26), phone: + 48 12 664 61 55
Mgr Aleksandra Kociniak, room: C025 (2.01.26), phone: + 48 12 664 61 55

Research topics

  • Molecular mechanisms of eukariotic gene transcription regulation by Yin Yang 1 and Yin Yang 2 (YY1 and YY2)
  • Influence of the cellular environment on the structure and function of YY1
  • Thermodynamics of molecular recognition in a model system: recombinant lipocalin – ligand (role of ionization, hydration, dimerization)
  • Obtaining new beta-lactoglobulin variants with given properties (increasing stability, changing the quaternary structure, increasing the affinity to selected ligands)
  • Mechanisms activating the signal transduction pathways involving the GPCRs and G proteins
  • Mechanism of formation of the signal platforms for GPCRs and G proteins with biomembranes
  • Role of lipids in signal transduction from GPCRs
  • Role of the membranes in homo- and hetero oligomerization of GPCRs
  • Oligomerization of GPCRs: influence of anti-psychotic drugs
  • Interaction between nanoparticles and target cells – optimizing nanocarriers for controlled transport of therapeutic agents
  • Optimization of nanocarriers for transporting therapeutic agents through the blood-brain barrier
  • Preparation of directed ligands for targeted drug transport
  • Studies on anti-cancer properties of LCS10 mixture
  • Proteomic studies of human nervous cells
  • Studies of antidepressant and antipsychotic drug in animal models (rat brain) and on human cells
  • Impact of selected gene silencing on the proteome of human nervous cells and their response to antidepressant and antipsychotic drug

Methods and specialized equipment

  • Molecular biology techniques: cloning, mutagenesis
  • Recombinant protein production and purification: New Brunswick Innova 43R, Amersham, ÄktaExplorer
  • Confocal microscopy (FRET-FLIM, FRAP)
  • Isothermal and differential microcalorimetry (ITC, DSC): MicroCal, CSC 6100
  • Spectroscopic methods (circular dichroism, steady-state and time resolved fluorescence, fluorescence anisotropy, FRET): Jasco J-170, Horiba, system 5000U
  • Fast kinetics techniques (T-jump, stopped-flow): Applied Photophysics SX-17 MW, Hi-Tech Scientific PTJ-64
  • Studies on protein-DNA interaction: EMSA, fluorescence anisotropy, sequence analysis
  • Liquid chromatography combined with tandem mass spectrometry in complex proteomic analyzes (LC-MS / MS) – sample preparation, design of proteomic experiments based on mass spectrometry, bioinformatic analysis of the obtained LC-MS / MS data
  • Interactomic and phosphoproteome studies
  • Culturing and differentiation of human nervous cells
  • CRISPR/Cas9 gene silencing in human nervous cells
  • Detection of proteins with immunoassays in human nervous cells: Western Blot, immunocytochemistry, subcellular imaging combined with flow cytometry as well as mRNA level testing by q-PCR

Current projects

  1. Agnieszka Polit: The effect of membrane domains on the G protein-lipid interaction (2017–2021). OPUS 12, National Science Centre (NCN).
  2. Sylwia Kędracka-Krok: Characteristics of clozapine and risperidone at the level of the cell nucleus (2018–2021). OPUS 13, National Science Centre (NCN).

Selected publications

  1. Stepien P, Augustyn B, Poojari C, Galan W, Polit A, Vattulainen I, Wisniewska-Becker A, Rog T, Complexity of seemingly simple lipid nanodiscs. BBA – Biomembranes 2020, 11, 83420.
  2. Bonarek P, Loch JI, Tworzydło M, Cooper DR, Milto K, Wróbel P, et al., Structure-based design approach to rational site-directed mutagenesis of β-lactoglobulin. J Struct Biol. 2020 (210) 107493. 
  3. Skupien-Rabian B, Jankowska U and Kedracka-Krok S. Analysis of a Nuclear Intrinsically Disordered Proteome. Methods Mol Biol. 2020;2175:181-196.
  4. Mystek P, Rysiewicz B, Gregrowicz J, Dziedzicka-Wasylewska M, Polit A. Gγ and Gα identity dictate a G-protein heterotrimer plasma membrane targeting. Cells 2019 8, 1246.
  5. Łukasiewicz S, Fic E, Bzowska M, Dziedzicka-Wasylewska M. Isolation of human monoclonal scfv antibody specifically recognizing the D2-5-HT1A heteromer. J New Dev Chem 2019 2:18-25.
  6. Łukasiewicz S, Stachowicz A, Fic E, Błasiak E, Kowalik A, Dziedzicka-Wasylewska M. Different strategies used in the purification of human monoclonal scfv antibodies. J Biol Med 2019 3:014-020.
  7. Figiel M, Łakomska J, Miłek P, Dziedzicka-Wasylewska M, Górecki A. The transcription factor YY2 has less momentous properties of an intrinsically disordered protein than its paralog YY1. FEBS Lett. 2019 Jul;593(14):1787-1798.
  8. Bonarek P, Polit A. Systematic calorimetric studies of proton exchange associated with binding of beta-lactoglobulin with ligand. Int J Biol Macromol. 2018 Dec;120:128-134.
  9. Loch JI, Bonarek P, Tworzydło M, Łazińska I, Szydłowska J, Lipowska J, et al., The engineered β-lactoglobulin with complementarity to the chlorpromazine chiral conformers, Int. J. Biol. Macromol. 2018 114: 85–96. 
  10. Kolasa M, Solich J, Faron-Górecka A, Żurawek D, Pabian P, Łukasiewicz S, Kuśmider M, Szafran-Pilch K, Szlachta M, Dziedzicka-Wasylewska M. Paroxetine and Low-dose Risperidone Induce Serotonin 5-HT1A and Dopamine D2 Receptor Heteromerization in the Mouse Prefrontal Cortex. Neuroscience. 2018 377:184-196
  11. Kedracka-Krok S, Swiderska B, Bielecka-Wajdman AM, Prus G, Skupien-Rabian B, Jankowska U, Obuchowicz E. Impact of imipramine on proteome of rat primary glial cells. J Neuroimmunol. 2018 Jul 15;320:25-37.
  12. Górka AK, Górecki A, Dziedzicka-Wasylewska M. Site-directed fluorescence labeling of intrinsically disordered region of human transcription factor YY1: The inhibitory effect of zinc ions. Protein Sci. 2018 Feb;27(2):390-401.
  13. Figiel M, Górecki A. Physical Interaction of Human Yin Yang 1 Protein with DNA. Crit Rev Oncog 2017 22(1-2):75–97.
  14. Łukasiewicz S, Błasiak E, Szczepanowicz K, Guzik K, Bzowska M, Warszyński P, Dziedzicka-Wasylewska M. The interaction of clozapine loaded nanocapsules with the hCMEC/D3 cells - In vitro model of blood brain barrier. Colloids Surf B Biointerfaces. 2017 1:200-210.
  15. Łukasiewicz S, Błasiak E, Szafran-Pilch K, Dziedzicka-Wasylewska M. Dopamine D2 and serotonin 5-HT1A receptor interaction in the context of the effects of antipsychotics  in vitro studies. J Neurochem. 2016 137:549-560.

Requirements for candidates

  • Basic knowledge on structural biochemistry
  • Basic knowledge on molecular biology and  protein engineering
  • Basic knowledge on protein production and purification
  • Basic knowledge on proteomics

Bachelor/master thesis topics

  • Structural analysis of the Pho protein from D. melanogaster
  • Functional analysis of YY1 protein mutants
  • Influence of molecular crowding on structure and function of human YY1 protein
  • Role of hydration in molecular recognition of recombinant lactoglobulin by selected ligands
  • Influence of stable dimerization on ligand binding by lactoglobulin
  • Purifying recombinant lactoglobulin from inclusion bodies
  • Preparation of a resin with immobilized beta-lactoglobulin
  • Optimizing production and purification of recombinant membranę proteins from GPCR family
  • Role of lipid membranes in signal cascades from G proteins and human neurotransmitter receptors (confocal microscopy, FLIM-FRET)
  • Analysis of the composition of lipid bilayer on its interaction with G proteins
  • Preparing and characterizing directed ligands for controlled transport of therapeutic agents
  • Preparation of fusion proteins for studying oligomerization of GPCRs
  • Analysis of GPCR oligomerization; influence of anti-psychotic drugs
  • Morphological, molecular and functional characterization of human nervous cell lines
  • Studies of antidepressant and antipsychotic drug in animal models (rat brain) and on human cells with use of advanced mass spectrometry techniques
  • Performing and verifying selected gene silencing  
In their master theses, students use genetic engineering to clone DNA, prepare efficient systems for protein overexpression in E. coli, Sf9 insect cells and human HEK293 cells, prepare fusion proteins and other protein mutants. Students take part in CRISPR/Cas9 gene silencing and preparing fusion proteins in neurons.  
In the structural studies, students employ stationary and time-resolved fluorescence measurements, circular dichroism spectroscopy, ITC and DSC microcalorimetry, stopped-flow kinetic analyses. 
In the proteomic studies, students take part in cell culture, cell visualization with microscopic techniques, immunoassays for particular proteins, preparation of samples for tandem mass spectrometry and LC-MS/MS data analysis. 

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Historical view

Professor Zygmunt Wasylewski (1942–2006)

Zygmunt Wasylewski was born in June 13th 1942 in Chrzanów. He finished elementary school there and in 1956 he started learning at a Mechanical Technical School. One year later he continued his education at a Chemical Technical School in Chorzów, where he obtained a secondary school diploma. 

In 1962–1968, he studied chemistry at the Faculty of Mathematics, Physics and Chemistry of the Jagiellonian University. He did his master's thesis under the supervision of Professor Włodzimierz Ostrowski in the Interdepartmental Chair of Physiological Chemistry at the then Krakow Medical Academy (now Collegium Medicum UJ). In this work, entitled "Determination of molecular parameters of phosphomonoesterase by molecular filtration", Zygmunt Wasylewski presented the values of effective Stokes radius, diffusion coefficient and molecular weight of phosphomonoesterase, determined experimentally. Then, for a year, Wasylewski worked as a scientific and technical assistant in the Department of Colloids, Faculty of Physical Chemistry, Mat-Physics-Chemistry Division, Jagiellonian University.

In 1969, he started work at the Department of Plant Physiology and Biochemistry of the newly established (1970) Institute of Molecular Biology at Jagiellonian University, directed by Professor Reifer. However, Professor Reifer’s research interests did not match those of the young master and in 1971 Z. Wasylewski moved to the Department of Animal Biochemistry of the same Institute, directed by Prof. Maria Sarnecka-Keller. Already two years later, Wasylewski defended his doctoral thesis entitled "Molecular Properties of various forms of acid phosphatases from liver and leukocytes", whose supervisor was Professor Aleksander Koj. In this work, using sophisticated chromatographic and electrophoretic techniques, as well as density gradient ultracentrifugation, Wasylewski, M.Sc., determined the degree of oligomerization of the molecules of the phosphatases studied and the geometry of the arrangement of protein subunits, and also demonstrated the structural similarity of acid phosphatases isolated from various tissues.

In his further research work, Dr. Wasylewski focused on interactions of model proteins with nonionic and ionic detergents, in particular with cationic detergents. In these studies he used a number of advanced physicochemical methods such as infrared spectroscopy techniques, Raman, EPR, hydrodynamic techniques such as gel filtration, ultracentrifugation and equilibrium dialysis. His independence and commitment resulted in an abundance of publications and a postdoctoral degree (habilitation) obtained in only six years (1979).

A new chapter in the scientific life of Dr. Wasylewski was opened by a one-year (1979/80) fellowship in San Antonio (Texas University), where he became interested in the application of fluorescence spectroscopy methods in the study of the structure, properties and dynamics of proteins. It should be emphasized that these methods allow for relatively easy study of proteins in aqueous solutions, thus being (besides NMR) a necessary complement to crystallographic methods.

Associate Professor Wasylewski (who received the title of associate professor in 1981) can be counted among the pioneers of the implementation of fluorimetric techniques in protein biochemistry. At that time, Wasylewski's "fluorescent" research focused on such enzymes as rhodanase, thiosulfate sulfotransferase, yeast hexokinase, alcohol dehydrogenase, metalloproteinase, phosphoglycerate kinase, human serine proteinase inhibitor and many other proteins containing two or more tryptophan residues. As a result of this work, in cooperation with Professor Horowitz, papers were published on temperature and ligand binding induced conformational changes of proteins in solution. Wasylewski's cooperation with Professor Efftink from the University of Mississippi (1986/87 for one year and in 1991 for three months as a visiting professor) was also conducive to further development in this field.

In 1986, docent Wasylewski and his research team developed a technique for decomposition of complex fluorescence emission spectra of multi-tryptophan proteins by fluorescence quenching-resolved-spectroscopy (FQRS). This technique is widely used today and has found its place in renowned textbooks on fluorescence spectroscopy.

In 1989, docent Wasylewski received the title of professor of biochemistry, and in 1991, the research group that had existed under his direction since the early 1980s (the Biopolymer Physicochemistry Laboratory within the Department of Animal Biochemistry) was transformed into the Department of Physical Biochemistry. The equipment base, still in Professor Wasylewski's laboratory at that time, was relatively rich, thanks to unparalleled constructional skills, persistence and enthusiasm of Professor Wasylewski, who designed devices, sought contractors for subassemblies of the designed apparatus far beyond the walls of the University, and then often screwed together and assembled individual elements with his own hands. It should be recalled that at that time there were almost no opportunities for the academic community to raise funds for the purchase of specialist equipment, but when the situation improved somewhat, i.e. around the middle of the 1990s, Professor Wasylewski immediately began his efforts to purchase high quality measuring equipment.

Initially, Professor Wasylewski's research interests were focused on the use of the FQRS method and other fluorescence techniques to study the molecular dynamics of proteins (e.g. parvalbumin, melittin) in solution, but also in model systems of biological membranes and in micelles. At that time, he investigated the mechanisms of fluorescence quenching, the red edge effect and the qualitative and quantitative analysis of fluorescence emission spectra. A little later, however, the main subject area of the Department of Physical Biochemistry crystallized. It concerned the influence of binding of functional ligands by bacterial regulatory proteins on the structure, dynamics and function of these proteins. Professor Wasylewski's research objects were proteins regulating transcription processes in E. coli, i.e.: tryptophan operon repressor (TrpR), tetracycline repressor (TetR) and cAMP-binding protein (CRP). Studies coordinated by Professor Wasylewski on the tryptophan repressor using a modified protein completely lacking tryptophan residues allowed to determine the nature of the L-tryptophan-locating microenvironment in the protein and also showed significant changes in the L-tryptophan-binding pocket area under the influence of binding of the TrpR-L-tryptophan complex to DNA. These studies used the FQRS technique, as well as steady-state and time-resolved tryptophan fluorescence emission measurements, and circular dichroism measurements. Parallel studies of the tetracycline repressor using the same measurement methods and protein mutants containing single tryptophan moieties enabled to understand the conformational dynamics of the protein domain responsible for interaction with DNA and to characterize the structural changes of TetR domains occurring as a result of protein interaction with tetracycline or operator DNA fragments. In turn, the application of the stopped-flow method with fluorescence detection allowed to characterize the kinetic mechanism of TetR protein interaction with DNA, as well as to describe kinetically the process of induction of expression of genes encoding resistance proteins under the influence of tetracycline binding, as well as to determine the role of magnesium ions in the induction process. The application of the isothermal calorimetric titration (ITC) method made it possible to understand the thermodynamics of the TetR-tetracycline interaction, while on the basis of data obtained by differential scanning calorimetry (DSC) a model of the TetR thermal denaturation process was proposed and the effect of tetracycline on protein stability was characterized.

The most extensive and probably the most valuable part of Professor Wasylewski's scientific output are works on CRP protein. The adventure with CRP began, one could say innocently, with the characterization of fluorescent properties of the protein. However, later, not easy kinetic studies using the stopped-flow technique made it possible to learn about the stability and kinetics of protein folding and unfolding, while the use of selective fluorescent labeling of cysteine residues made it possible to propose a detailed mechanism of chemical denaturation of CRP protein. The realization of Professor Warmus's ideas concerning further research on the function and structure of CRP protein required the introduction of many point mutations in "sensitive" areas of the protein. The realization of this last goal was as much a challenge as it was an appealing prospect. Thanks to Professor's steadfastness in pursuing his goal, a molecular biology laboratory was established within the Department of Physical Biochemistry, one of the first in the Institute of Molecular Biology, where, using the overlap extension PCR method, mutations were introduced and then verified by DNA sequencing. The intensity of research conducted on multiple mutants of CRP protein necessitated modification of bacterial culture and protein purification techniques. This resulted in the introduction of advanced affinity chromatography methods into laboratory procedures and automation of protein preparation, made possible by the use of a biofermenter and a specialized chromatographic system. The use of mutants allowed monitoring of ligand-induced allosteric changes in CRP, thanks to which the detailed kinetic mechanism of cAMP binding was described. In parallel, comprehensive structural studies (using DLS, FRET, fluorescence quenching, steady-state and time-resolved emission and fluorescence anisotropy measurements) were carried out to describe conformational changes in the protein induced by its interaction with cAMP and DNA. In turn, the thermodynamics of CRP-cAMP complex formation were studied using microcalorimetric methods (ITC, DSC). Since the crystallographic structure of the CRP protein not complexed with the ligand has not been known so far, there has been a discussion in the scientific community on the structural symmetry of the homodimer subunits. In the context of the arising research problem, a new unusual idea of Professor Wasylewski was born, concerning the construction of CRP protein heterodimer having only one tryptophan residue. The results of studies of cAMP binding kinetics monitored by energy transfer between the Trp residue and a fluorescent tag attached to a cysteine residue located in the same as Trp or in the second subunit of the protein showed the conformational symmetry of the CRP protein subunits.

The culmination of the CRP work was a project to investigate the interactions between elements of the entire E. coli transcriptional complex using selected promoter DNA fragments. This challenging project required the reconstitution of RNA polymerase from purified recombinant protein subunits. The formation of the transcription complex, which included a CRP-cAMP complex in addition to the RNA polymerase, was monitored by measuring the fluorescence anisotropy of fluorescently labeled DNA fragments. As a result, the effect of CRP on specific and nonspecific RNAP-DNA interactions was determined. Furthermore, the use of time-resolved fluorescence spectroscopy (FRET, fluorescence anisotropy) enabled the study of the conformational dynamics of transcription complexes.

Professor Wasylewski was fascinated by technical discoveries in the field of physical biochemistry and molecular engineering, with which the end of the 20th century was exploding. He not only followed them, updating his knowledge, but also used them practically as useful tools in his everyday work. Professor Wasylewski's talent as a designer, as well as his pragmatic personality, were once again evident when, entering completely new areas of research, he began to study the interactions between human neurotransmitter receptors in plasma membranes. The assumptions about their heterodimerization were confirmed experimentally for the first time thanks to him, and it should be emphasized that the competition in this field of science is enormous. The experiments consisted of measuring the fluorescence lifetimes of fluorescent proteins bound to receptors in a single living cell and required the use of sophisticated apparatus, which, however, could not be afforded. The need to answer this question was so urgent for Professor Wasalewski that he created a functional measuring system using components available in his laboratory.

The last year of Professor Wasylewski's life was dominated by the work on the formation of two completely new scientific projects. One of them concerned the human regulatory protein Ying-Yang1 and was a certain analogy and extension of the research conducted on the bacterial CRP protein. The other one concerned the application of genomics and proteomics methods to study the influence of antidepressant drugs on the protein profile of neuronal cells.This stage ended with a full success manifested by obtaining the financial support needed to carry out both of the intended tasks.

Professor Wasylewski was the principal investigator of four three-year research projects and is the author or co-author of about sixty scientific publications. In 1991 he was awarded the Knight's Cross of the Order of Polonia Restituta, and in 2002 he received the title of full professor. He was also a member of the Polish Biochemical Society, and from the early 1990s he was a member of the molecular biology, biochemistry and biophysics section of the Scientific Research Committee on several occasions. 

Another very important aspect of Professor Wasylewski's professional activity was his didactic work. As an assistant, he conducted laboratory classes as part of a specialized biochemistry lab. Later, already as an assistant professor (1973), he also taught instrumental analysis in biochemistry. In 1980, Associate Professor Wasylewski began lectures in physical biochemistry, which were closely correlated with laboratory classes conducted by the staff of his Laboratory. After the formation of the Laboratory of Molecular Biology, in 1998, he introduced a course on protein engineering, which included both practical classes and lectures. The latter course in particular is of great interest to students as it comprehensively addresses the issue of obtaining protein mutants, starting from manipulation at the DNA level, through protein isolation, to determining its basic structural properties and checking its biological activity. With the introduction of biochemistry specialization in the Biotechnology faculty, two highly advanced courses were created: Physical Biochemistry II and Protein Engineering II. Professor Wasylewski was the supervisor of 13 doctoral theses and dozens of master's theses, he was also a reviewer of many scientific papers and research projects.

Professor Wasylewski was always kind to his students, he always had time for them and, what was rare, he bestowed a great deal of trust on the young people coming to the Department. He was able to attract students in many ways. In some of them, he aroused keen interest in the subject matter or methodology, in others he infected with scientific enthusiasm and in yet others he charmed with his openness and personal charm. One student, when asked by Professor Wasylewski what she would like to do in her Master thesis, replied: "I would like to clone Mozart", to which Professor replied: "That is what we are doing". This anecdote reveals one important quality of Professor Wasylewski: he was a visionary who set goals that for others could only remain in the realm of dreams and, without hesitation, strove to achieve them. He liked to surround himself with young people who were able to share his enthusiasm and optimism. Analyzing his scientific development, one can clearly see the evolution of the subject matter, which became more and more complex, but also more important, more interesting and, at the same time, more difficult.

Professor Wasylewski's professional life was inseparably intertwined with the life of the Institute of Molecular Biology (Faculty of Biology and natural Sciences, Jagiellonian University). In 1981–1984 he held the position of the Institute's Deputy Director for didactics, and in 1997–2003 he was the director of doctoral studies. He was a co-founder of the Faculty of Biotechnology and participated in the process of separation of the Faculty of Biotechnology from the Faculty of Biology and Natural Sciences UJ (2002). On several occasions, he made efforts to establish a major in Biochemistry, being deeply convinced of the need to strengthen the condition of his beloved discipline of science. These efforts unfortunately ended in failure and remained an unfulfilled dream of the Professor (it came true in the following years).

Professor Wasylewski was a man who had the good of his country at heart, as evidenced by his involvement in opposition activities during martial law (1981–1984) and later. He was one of the six members of the University's Secret Commission of Solidarity. This committee, composed of recommended members of the official Solidarity structure, was an expression of opposition of the academic community to the mistreatment they experienced from "people of the system". It operated from 1982 to 1988, and its main tasks were: breaking the monopoly of information of the "system" through the distribution of underground press, assistance to repressed scientists, as well as internal control of the university authorities by giving opinions on candidates for important positions. The activity of the Commission involved considerable risk, which its members were aware of, but their sense of duty to the University and their country, and above all their sense of dignity, made them take this risk. Interestingly, for some time the meetings of the Commission were held in Professor Wasylewski's apartment. Later, the Secret Intercollegiate Commission was established, in which Professor Wasylewski represented the Jagiellonian University. These important facts from the life of the University still await description, as do other, not always glorious, details from that difficult period, but – what sounds promising – has recently become the object of research by a special Senate Committee of the Jagiellonian University.

Professor Wasylewski was an extremely energetic man, eternally young in spirit but also very physically fit. Skiing was his passion and he was indeed an excellent skier, as participants in the Institute's annual winter schools could see for themselves. He was an exceptional man, combining seemingly contradictory features of a pragmatist and an idealist. Future-oriented, cheerful, family-oriented, and simply human, he passed away suddenly, in the prime of his life, leaving his colleagues and friends in grief.

Collected by: Sylwia Kędracka-Krok



Dr hab. Sylwia Łukasiewicz, December 10, 2019

Dr hab. Andrzej Górecki, May 21, 2019

Dr hab. Sylwia Kędracka-Krok, February 26, 2017


Dr. Paweł Mystek, April 10, 2018 

Dr. Adam Górka, November 13, 2018

Dr. Urszula Jankowska, December 20, 2016

Dr. Małgorzata Figiel, May 13, 2016

Dr. Ewa Błasiak, October 9, 2015

Dr. Filip Gołębiowski, November 30, 2012

Dr. Anna Kwasek, June 17, 2011

Dr. Sylwia Łukasiewicz, March 27, 2009

Dr. Ewelina Fic, October 30, 200

Dr. Piotr Bonarek, November, 2006 

Dr. Andrzej Górecki, June 30, 2006 

Dr. Sylwia Kędracka-Krok, May 7, 2004 

Dr. Magdalena Tworzydło, March 5, 2006 

Dr. Urszula Błaszczyk, March 21, 2003

Dr. Agnieszka Polit, December 3, 2002

Dr. Andrzej Guz, April 26, 2002

Dr. Zofia Blicharska, January 25, 2000

Dr. Jędrzej Małecki, November 16, 1999


Master thesis

Academic year 2019/2020

  • Paulina Borkowska (Biochemia)
  • Krzysztof Pierzchała-Lichwa (Biochemia)

Academic year 2018/2019

  • Agata Cieślik (Biotechnologia molekularna)
  • Agata Kowalik (Biotechnologia molekularna)
  • Adrianna Próba (Biochemia)
  • Katarzyna Lichańska (Biochemia)
  • Filip Szubert (Biotechnologia molekularna)
  • Aleksandra Rzeszuto (Biochemia)
  • Tomasz Pasionek (Biofizyka)
  • Joanna Pyrzewicz (Biochemia)

Academic year 2017/2018

  • Beata Rysiewicz (Biochemia)
  • Przemysław Dutka (Biochemia)
  • Marta Kluz (Biotechnologia molekularna)
  • Dorota Mularczyk (Biofizyka)
  • Mateusz Szwalec (Biofizyka)
  • Piotr Miłek (Biotechnologia molekularna)
  • Ahmed Hal (Molecular Biotechnology)

Academic year 2016/2017

  • Antoni Mikołajczyk (Biochemia)
  • Filip Pamuła (Biochemia)
  • Maciej Gacek (Biochemia)
  • Alicja Cieślewicz (Biofizyka)
  • Julia Łakomska (Biochemia)
  • Magdalena Pilch (Bichemia)
  • Cyntia Kubicka (Biochemia)
  • Kajetan Sawa (Biotechnologia molekularna)

Academic year 2015/2016

  • Zuzanna Pakosz (Biofizyka)
  • Dawid Deneka (Biotechnologia)
  • Katažyna Milto (Biochemia)
  • Gabriela Pruś (Biochemia)

Rok akademicki 2014/2015

  • Anna Nieborak (Biotechnologia)
  • Paweł Bąk (Neurobiologia)

Rok akademicki 2013/2014

  • Ertugrul Anmak (Biotechnology in English)
  • Karolina Wojciechowska (Biotechnologia)
  • Katarzyna Buczak (Biochemia)

Academic year 2013/2014

  • Anna Baranowska (Biochemia)
  • Viktoriya Kurylsto (Biotechnologia)
  • Aleksandra Niedbałowska (Biotechnologia)
  • Kinga Nytko (Biotechnologia)
  • Agata Stachowicz (Biotechnologia)
  • Katarzyna Wajda-Nikiel (Biotechnologia)
  • Dawid Żyła (Biotechnologia)

Rok akademicki 2012/2013

  • Michał Ciepiela (Biochemia)
  • Jakub Lenard (Biotechnologia)
  • Anna Piotrowska (Biochemia)
  • Piotr Stępień (Biofizyka)
  • Mateusz Wilamowski (Biofizyka)

Academic year 2011/2012

  • Anna Chmielińska (Biochemia)
  • Andrzej Galiński (Biotechnologia)
  • Paweł Mystek (Biofizyka)
  • Agnieszka Skupień (Biotechnologia)
  • Bożena Skupień-Rabian (Biotechnologia)
  • Mateusz Śledź (Biotechnologia)
  • Bianka Świderska (Biotechnologia)

Academic year 2010/2011

  • Michał Cnota (Chemia)   
  • Mateusz Dyla (Biochemia)
  • Dominika Olszewska (Chemia) 
  • Barbara Sierpień (Biotechnologia)
  • Dominika Szot (Chemia)
  • Klaudyna Śpiewak (Chemia)

Academic year 2009/2010

  • Adam Górka (Biotechnologia)
  • Roman Kityk (Biotechnologia)
  • Kamila Miłkowska (Biotechnologia)
  • Barbara Mojsa (Biotechnologia)
  • Małgorzata Olech (Biotechnologia)
  • Artur Piróg (Biotechnologia)
  • Piotr Skrobecki (Chemia)
  • Jakub Tomasik (Biotechnologia)

Academic year 2008/2009

  • Damian Dawidowski (Biotechnologia)
  • Ewa Kowalczyk (Biotechnologia)
  • Justyna Kuśmierczyk (Biotechnologia)
  • Lech Moczulski (Biotechnologia)
  • Katarzyna Smaga (Biofizyka)

Academic year 2007/2008

  • Marcin Cieślik (Biotechnologia)
  • Dominika Gruszka (Biotechnologia)
  • Marcin Jaciuk (Biotechnologia)
  • Urszula Jankowska (Biotechnologia)
  • Aleksandra Kałużny (Biotechnologia)
  • Lucyna Ślusarz (Biotechnologia)
  • Katarzyna Zabłocka (Biotechnologia)
  • Karolina Zielińska (Biotechnologia)

Academic year 2006/2007

  • Marta Blamowska (Biotechnologia)
  • Anna Cieślińska (Biotechnologia)
  • Magdalena Gąska (Biotechnologia)
  • Filip Gołębiowski (Biotechnologia)
  • Jadwiga Oczoś (Biotechnologia)

Academic year 2005/2006

  • Ewa Błasiak (Biotechnologia)
  • Anna Dziecichowicz (Fizyka medyczna)
  • Jakub Gruszczyk (Biotechnologia)
  • Lech Kaczmarczyk (Biotechnologia)
  • Przemysław Łabuz (Biotechnologia)
  • Alina Mazur (Chemia)
  • Justyna Wojdyła (Biotechnologia)

Academic year 2004/2005

  • Łukasz Idec (Biotechnologia)
  • Renata Kubiczek (Biologia)
  • Eliza Płoskoń (Biotechnologia)

Academic year 2003/2004

  • Joanna Andrecka (Biotechnologia)
  • Paweł Hodurek (Biotechnologia)
  • Anna Jasiak (Biotechnologia)
  • Magdalena Zaniewska (Biotechnologia)

Academic year 2002/2003

  • Aleksandra Mikołajka (Biotechnologia)
  • Sylwia Łukasiewicz (Biotechnologia)
  • Lech Wojakiewicz (Biotechnologia)

Academic year 2001/2002

  • Magdalena Budzowska (Biotechnologia)
  • Anna Chrostek (Biotechnologia)
  • Ewelina Fic (Biotechnologia)
  • Agnieszka Gambuś (Biotechnologia)
  • Stella Koprowska (Biologia)

Academic year 2000/2001

  • Anna Kłapyta-Kwasek (Chemia)
  • Wojciech Piwko (Biotechnologia)

Academic year​ 1999/2000

  • Przemysław Błyszczuk (Biotechnologia)
  • Paweł Śmiałowski (Biotechnologia)