Infrared spectroscopy can trace out various modifications in protein structure

Infrared (IR) spectroscopy is a frequently used technique for the structural analysis of simple and complex molecules.

It has wide applications in both the qualitative and quantitative analysis of proteins in different samples. The technique provides a clear picture of primary, secondary or tertiary structure of a protein to biochemists.

Infrared radiation is useful in assessing different vibrational modes which arise from variations in the structural components of a protein.

This review, written by Dr. Rohit Bhatia, ISF College of Pharmacy, Ferozepur, India, presents a report of different studies published around the world on the use of IR spectroscopic techniques to elucidate protein structure and function.

The review explains the basics of IR spectroscopic techniques alongside the observed trends in their use in protein chemistry. The reviewers have presented the information with the help of informative tables that can benefit researchers by providing a handy summary when designing their own experiments.

The team has observed that fourier transform infrared spectroscopy (FTIR) 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 inorganic materials. It is also evident it can be utilized to quantify the proteins in variety of samples.

The review presents a brief but informative summary of different types of IR spectroscopic methods, numerical parameters for experimentation, sampling techniques, their advantages and disadvantage as well as recent advances. Recent findings about protein content in different types of food and natural samples are also explained.