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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.

In order to study protein structure and function, we use Fourier Transform Infrared (FT-IR) Spectroscopy.  Infrared (IR) spectroscopy, probing 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).

Information about protein secondary structure is revealed in the Mid-IR region (some representative spectra are shown below), more specifically in the fingerprint region: 1800- 1300 cm-1.

To contact us:

Biophysics logo

Atılım University, İncek Kampüsü

Mühendislik Fakültesi, Fizik Grubu

Biyofizik Laboratuvarı, No: B-2021

Kızılcaşar Mh. İncek 06836 Gölbaşı, Ankara

Office Tel.: +90-312 586 8319

Lab. Tel.: +90-312 586 8552

Structure comparison of OmpG-16S mutant at different pH. Shown IR spectra cover the fingerprint region, i.e., 1800-1300 cm-1.

Side chain modes and the result of subtraction (black) of these modes from the raw spectrum (blue).

Structure comparison of OmpG-16S mutant in H2O and D2O buffer.

Page last updated: 10.11.2017

Biophysics Laboratory was established through the Research Laboratory Projects (ALP) program sponsored by Atılım University.

Laboratory