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Progress in Infrared Spectroscopy as an Efficient Tool for Predicting Protein Secondary Structure

February 22, 2022

International Journal of Biological Macromolecules | February 22, 2022

Shouning Yang  Qiaoling  Zhang, Huayan Yang, Haimei Shi, Aichun Dong, Li Wang, Shaoning Yu

Int J Biol Macromol
. 2022 Feb 22;206:175-187.

DOI: 10.1016/j.ijbiomac.2022.02.104.


Infrared (IR) spectroscopy is a highly sensitive technique that provides complete information on chemical compositions. The IR spectra of proteins or peptides give rise to nine characteristic IR absorption bands. The amide I bands are the most prominent and sensitive vibrational bands and widely used to predict protein secondary structures. The interference of H2O absorbance is the greatest challenge for IR protein secondary structure prediction. Much effort has been made to reduce/eliminate the interference of H2O, simplify operation steps, and increase prediction accuracy. Progress in sampling and equipment has rendered the Fourier transform infrared (FTIR) technique suitable for determining the protein secondary structure in broader concentration ranges, greatly simplifying the operating steps. This review highlights the recent progress in sample preparation, data analysis, and equipment development of FTIR in A/T mode, with a focus on recent applications of FTIR spectroscopy in the prediction of protein secondary structure. This review also provides a brief introduction of the progress in ATR-FTIR for predicting protein secondary structure and discusses some combined IR methods, such as AFM-based IR spectroscopy, that are used to analyze protein structural dynamics and protein aggregation.

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