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Raman Spectral Analysis in the C−H Stretching Region of Proteins and Amino Acids for Investigation of Hydrophobic Interactions

Howell, Nazlin K., Arteaga, Guillermo, Nakai, Shuryo, Li-Chan, Eunice C. Y.·1999·Journal of Agricultural and Food Chemistry

Abstract

Raman spectra of amino acids showed complexity in the C-H stretching region (2800-3100 cm(-)(1)) attributed to diversity of CH, CH(2), and CH(3) groups in the side chains, ionization state, and microenvironment. The involvement of specific amino acids in the C-H stretching region of selected proteins, namely, lysozyme, alpha-lactalbumin, beta-lactoglobulin, and their binary mixtures, was investigated by deconvolution using maximum likelihood techniques. The main protein band near 2940 cm(-)(1) was attributed not only to aromatic and aliphatic amino acids but also to many other amino acids. A band near 3065 cm(-)(1) was assigned to aromatic residues, whereas bands near 2880 and 2900 cm(-)(1) corresponded primarily to aliphatic amino acids. Heating at 90 degrees C increased relative intensity near 2940 cm(-)(1) and decreased relative intensity at 2895-2902 cm(-)(1) for lysozyme and its mixtures with alpha-lactalbumin or beta-lactoglobulin. Additional bands at 2812 or 2838 and 3003 cm(-)(1) were observed after heating or in 8 M deuterated urea, reflecting changes upon denaturation.

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Metadata

Authors
Howell, N. K., Arteaga, G., Nakai, S., & Li-Chan, E. C. Y.
Venue
Journal of Agricultural and Food Chemistry
Published
1999-02-02
Volume
47
Issue
3
Pages
924-933
ISSN
  • 0021-8561 (ISSN-L)
  • 1520-5118
OpenAlex
W2076601495
Cited by
220
References
0
FWCI
1.65
Type
journal article
Language
en
Open access
closed

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Howell, N. K., Arteaga, G., Nakai, S., & Li-Chan, E. C. Y. (1999). Raman Spectral Analysis in the C−H Stretching Region of Proteins and Amino Acids for Investigation of Hydrophobic Interactions. Journal of Agricultural and Food Chemistry. https://doi.org/10.1021/jf981074l

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