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 the primary, secondary, or tertiary structure of a protein. Infrared radiations are used to assess different vibrational modes 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. They were further studied thoroughly and important findings/ data were compiled and represented with tables and figures. The procured data, which includes bandwidth, frequency and intensity, have been employed to elucidate the structure of a protein.
Results: It was found from various reports that Fourier transforms infrared spectroscopy (FT-IR) has widely been utilized to predict the secondary structure of the protein in the past few years. FTIR has the ability to trace out various structural modifications in the protein structure that originate due to interactions with other materials. It is also evident that it can be utilized to quantify the proteins in a variety of samples.
Conclusion: The present review describes the basic principle and the instrumentation of IR spectroscopy and its advancements. Beyond this, various applications of this technique in determining protein structure and quantification in different materials such as food stuffs, biotechnological products and biological fluids have also been summarized.
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