Turku Bioscience P.O. Box 123, BioCity
(Street addr. Tykistökatu 6 B)
FIN-20521 Turku, Finland
Phone: +358 2 333 8012
FAX: +358 2 333 8000
We use X-ray crystallography as the major tool to provide detailed information on the structure and function of biological molecules. Knowledge of the 3-dimensional structure of proteins is essential to understand at the atomic level how proteins function or, in the case of diseases, how they malfunction. Our current projects include:
- Pathogen-host interactions
The complexity of pathogen-host interactions is investigated in our group by looking at proteins involved in stress protection and adhesion. Understanding the mechanistic details of bacterial survival under various forms of stress could be useful in the design of novel ways to combat or prevent disease. Peroxide resistance, for example, plays a major role in the survival of bacteria and the spread of disease. We are particularly interested in a class of ferritin-like proteins that are able to bind and oxidize iron. By combining site-directed mutagenesis, protein structure determination and X-ray absorption spectroscopy we aim to provide a more comprehensive view of the role and function of ferritin-like proteins in bacterial survival. Adhesion offers alternative solutions to combat antibiotic resistance and we are currently working on newly identified proteins to provide structural insights for the design of new antibacterial strategies.
- Signalling proteins
Signalling is a biological process that depends strongly on molecular recognition and protein-protein interactions. Our aim is to understand the structural aspects of this process at atomic level and to use the obtained structural information for the development of novel ways of therapeutic intervention in disease.
- Enzyme structure and function
Understanding enzyme adaptation in various environmental conditions will enable the design of better performance tailor-made enzymes for use in biomedicine, biotechnology, and green chemistry. Structure determination at high/atomic resolution combined with directed evolution, mutagenesis studies, thermal denaturation analysis and other biophysical techniques is expected to give a better picture of the studied proteins/enzymes under various conditions. Thus, for protein stability studies we use a multidisciplinary approach that includes, apart from X-ray crystallography, several biophysical methods such as fluorescence spectroscopy, microcalorimetry, circular dichroism, and enzyme kinetic assays.
- Radiation damage
The use of synchrotron radiation has been central to all our structural studies. By analyzing data collected in synchrotrons followed by close inspection of the resultant protein structures at atomic resolution we have been able to study more fundamental problems in crystallography, such as radiation damage. The latter arises from the interaction of powerful X-rays with biological specimens and has become a critical issue in modern data collection strategies. Understanding this process and finding ways to prevent it is important for the elucidation of more accurate protein structures.