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EU Innovative Training Network ES-Cat

Hannes Konegger


The start of my academic development goes back to the University of Natural Resources and Life Sciences in Vienna, where I studied Food Science and Biotechnology. I concluded my bachelor studies in the lab of Prof. Florian Rüker, where I gained fundamental insights into the field of protein engineering. Within the scope of my subsequent master study in Biotechnology, my main interests manifested around protein chemistry, molecular biology and environmental biotechnology.
This furthermore led me to two external collaborations. In 2013, I was investigating the effects of high salinity on the growth and the biomass yield of selected green algae at The Energy and Resources Institute in New Delhi, India.
Later, a scholarship awarded by the Industriellenvereinigung Kärnten as well as funding from the Erasmus+ Programme gave me the opportunity to conduct research on the engineering of the [FeFe]-Hydrogenase HydA1 from Chlamydomonas reinhardtii in the lab of Prof. Thomas Happe at the Ruhr-University Bochum in Germany. This project involved the application of a semi-rational directed evolution approach to investigate the electron transport characteristics of the enzyme.

Training and Transferable Skills:

  • Analytical Chemistry (high performance liquid chromatography, gas chromatography)
  • Biochemistry (expression & characterization of proteins, establishment of screening assays)
  • Bioinformatics (phylogenetics, multiple sequence alignments, molecular dynamics)
  • Microbiology (green algae, bacterial & yeast cells cultivation, also anerobically)
  • Molecular Biology (cloning, polymerase chain reaction, generation of mutant libraries by site-saturation mutagenesis)

Research Projects:
One major factor precluding the potential usage of proteins within industrial or medical applications is the limited structural stability of these biomolecules, in particular encountered at environmental conditions beneficial for the intended purposes. Such stability bottlenecks at the same time restrict the evolvability of either novel or enhanced functionality, which in return complicates the engineering approach to emerge proteins to satisfy human needs.
To address some of these limitations, I will study in detail general principles and mechanisms driving unfolding processes in two unrelated proteins via the application of atomistic molecular dynamics simulations and enhanced sampling methods, e.g. metadynamics, accelerated molecular dynamics and Markov State Models. This theoretical approach will additionally be complemented by data derived from biophysical characterization, which facilitates the identification of relevant factors confering to increased (thermo)stabilities of proteins.
During the course of evolution, nature elaborated an inconceivable number of differing solutions to given problems under changing environmental conditions. This rich functional diversity is still encoded in DNA sequences spread over several branches of the tree of life. Phylogenetic reconstruction methods allow to access and process the exponentially growing DNA sequence databases, in order to reveal patterns which are representative for stable protein structures and folds. Thus, another aspect of my research will manifest as the analysis of the gathered insights, which may in return facilitate the process of engineering thermostability in a multitude of proteins.