Background: Infrared (IR) spectroscopy is a well established technique for the structural elucidation of simple
as well complex molecules. It has wide applications in the qualitative as well as quantitative determination of proteins in
different samples. It provides a clear picture of primary, secondary or tertiary structure of a protein. Infrared radiations are
used to assess different vibrational modes which arise from variations in the structural components of a protein.
Methods: Various research reports were collected from search engines like Sciencedirect, Pubmed, Researchgate and
Google Scholar. These were further studied thoroughly and important findings/data were compiled and represented with the
help of tables and figures. The procured data which includes band width, frequency and intensity has been employed to
elucidate the structure of a protein.
Results: It was found from various reports that fourier transform infrared spectroscopy (FT-IR) has been widely utilized for
prediction of secondary structure of protein in the past few years. FTIR has the ability to trace out various structural
modifications in the protein structure which arise due to interactions with other materials. It is also evident it can be utilized
to quantify the proteins in variety of samples.
Conclusion: The present review describes the basic principle and the instrumentation of IR spectroscopy along with its
advancements. Beyond this, various applications of this technique in determination of protein structure and quantification
in different materials such as foods stuffs, biotechnological products and biological fluids have also been summarized.