Monika Pranjic
Tell us something about your background.
I obtained a BSc in Molecular Biology and an MSc in Biochemistry and Molecular Biomedicine via an inter-university study programme between the University of Graz and Technical University of Graz. This cooperation offers a broad repertoire of specialisation in the study programme and I focused on Enzymology and Structural Biology. Within the frame of my Master Thesis “High throughput methods for hP450 engineering”, I started working in the field of biocatalysis, more specifically, high throughput screening methods and protein engineering of mono-oxygenase enzymes.
My academic career was complemented by several extra-curricular academic courses and research internships, one of these at the Institute of Pharmacology and Toxicology, Gießen, Germany, where I gained first experiences in protein engineering (Scientific Project: “Single Nucleotide Polymorphisms (SNPs) in human Sodium-Dependent Organic Anion Transporter (hSOAT)”). And I spent a term abroad for a period of eight months at the University of Technology of Compiègne, France, where I completed courses in the universities’ study programme of biological engineering.
Tell us a bit about your PhD project in OXYTRAIN and your research interests.
My project in OXYTRAIN: Study in the oxidative mechanism of action of the copper sites of lytic polysaccharide monooxygenases (LPMOs)
The project’s objective is to obtain new insight into the mechanism of the copper-oxygen active site of LPMOs, particularly aiming at elucidating their mechanism and augmenting the biocatalyst action. The expected results are, firstly, the characterisation of polysaccharide chemistry following LPMO action; secondly, the development of a SERS-assay for the study of LPMOs enabling the rapid evaluation of their oxidative activity; and thirdly, the trial of new copper catalysts as LPMO replacements.
I feel fortunate to undertake my PhD at the University of York with Professor Paul Walton and his research group, where the active site of LPMOs was discovered in 2011. This active site is known as the histidine brace and includes a copper-containing active site with an N-terminal N-methylated histidine. I am highly motivated to study the functionality of LPMOs further and to contribute to their structural clarification. In addition, I am looking forward to use new methodologies in the field of Structural Biology, EPR spectroscopy and Enzyme Kinetics.
What do you expect from OXYTRAIN?
The OXYTRAIN programme includes inter-disciplinary and scientific training that will improve my scientific and personal development in the course of a PhD. Moreover, I hope that the OXYTRAIN network will exploit the potential of a diverse enzymatic class for industrial applications and contribute to the enhancement of Green Chemistry and Biocatalysis in the future.
What do you like to do in your free time, your hobbies, interests, what motivates you.
There is a lot that I like to do, for one, travel. So during my educational career I attended several academic courses abroad and was working in an international student’s organisation, which allowed me to learn how to work in an international context and to meet people from all over the world.
My greatest hobby is Tae-Kwon-Do. Starting from an early age, I competed in different martial art tournaments and won several titles (latest 2016, Tae-kwon-Do Styrian Champion).
Against this background, I think that my motivation strives from values like curiosity, enthusiasm and perseverance. Curiosity and enthusiasm is what brought me to a scientific, research based career. And perseverance, as one of the philosophical principles of martial arts, is what keeps me motivated while facing hardships.