University of Patras
University Campus- Rio, PATRAS, PO: 26500 (Greece)
Such a state-of-the-art centre will create a research ecosystem providing a number of positions for highly skilled scientists, engineers and for other qualified staff, and thus enhance scientific and economic growth both at a local and at a regional level, which will hopefully be sustained for years to come. It will also achieve the optimal integration of UPAT’s Structural Biology in ERA through the establishment of long-lasting partnerships, and will enhance the exchange of expertise and the building of networks with other scientists and technology end-users at a regional or local level, including the biopharmaceutical industry. Last, but not least, UPAT will provide knowledge, expertise and access to national, regional European and extra-European users or groups.
Solution structure detrmination using NMR data and NMR-driven interaction studies monitored through 2D 1H-15N HSQC experiments. Secondary structure studies through Circular Dichroism
NMR targeted and non-targeted metabolomics
High-Yield expression of recombinant proteins for structural and functional studies. 15N, 13C & 2H uniform, selective and segmental labeling of proteins for NMR stduies. Purification of proteins and physicochemical Characterization
The UPAT’s upgraded Confocal Microscopy Facility, is up to our knowledge unique in Greece for its capacities, properties and applications. This set up will allow the integration of the information gained on drug-target structures following their functional characterization. Insights from structural determination will be validated in live cells, to allow an understanding of how the biomolecule tested affects basic cellular pathways at the molecular levels. In addition, novel bioactive molecules will be evaluated for their efficacy in modulating protein target function and its signaling pathways.
State of the art Circular Dichroism spectrometer, with capabilities for thermal unfolding/refolding of proteins
700 MHz NMR spectrometer with a cryogenically cooled probe for enhanced sensitivity and four channels, in concert with uniformly or selectively enriched recombinant proteins (in 13C, 15N and 2H), allows the set up of various applications in the field of structural biology and drug design.
A crystallization robot, unique in UPAT, is expected to provide new possibilities for crystallization trials and enhance efforts in Structure determination of proteins in crystals through X-ray diffraction.