The main focus of the Biophysics Laboratory is to investigate the structure-function relationship of proteins using FTIR Spectroscopy. Proteins are involved in every process within living cells. They perform a large variety of functions such as providing protecting functions, participating in transport processes, catalysis of all biochemical reactions within the cell and are basic substances of antibodies and certain hormones. Correct functionality of a protein depends on its structure and correct conformation. Therefore understanding the structure, function of proteins and conditions for functionality has been the focus of many scientific researches.
Fourier Transform Infrared (FT-IR) Spectroscopy is the leading spectroscopic method in our research for probing the structure, function and kinetics of proteins and enzymes. Infrared (IR) spectroscopy, monitoring the vibrational modes of molecules, is based on the interaction of electromagnetic radiation with the electric dipole moment of the molecule. IR spectroscopy is a non-invasive technique providing direct information on bond orders, electrostatic interactions, H-bonding, charge distributions, protonation states, redox states, dynamics and kinetics. The IR region covers the range between 0.7-500 μm (14000 and 20 cm-1) in electromagnetic spectrum. This region is divided into three groups as near-IR (0.8-2.5 μm or 12500-4000 cm-1), mid-IR (2.5-25 μm or 4000-400 cm-1) and far-IR (25-100 μm or 10-400 cm-1).