Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 164, Issue -, Pages 2753-2760Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2020.07.299
Keywords
FT-IR; Protein secondary structure; Gluten
Funding
- Ministry of National Education, Republic of Turkey
- Whistler Center for Carbohydrate Research
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Amide I and Amide III vibrational modes are frequently used to study protein secondary structure with Fourier transform infrared (FT-IR) spectroscopy. However, for protein mixtures, neither the sole Amide I nor Amide III region provides sufficient information for structural quantitation because of overlapping peaks, especially in the Amide I region. Here, an improved quantitative approach is proposed to estimate secondary structure of protein systems using resolution enhancement and curve-fitting data processing techniques on a gluten model system to investigate structure-function relationships. Twelve different scenarios were prepared to assign bands in the Amide I region. Frequency ranges of 1660-1640 cm(-1) and 1665-1660 cm(-1) were found to highly contribute to variability in secondary structure contents of samples. Utilization of the Amide III region as a conducive tool to assign bands in the Amide I region led to a better differentiation of some secondary structural motifs and a more accurate quantitation of protein secondary structure. The study presents an understanding of FT-IR data analysis for a quick technique to assess secondary structures of protein mixtures. (C) 2020 Published by Elsevier B.V.
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