Izvestiya of Saratov University.

Physics

ISSN 1817-3020 (Print)
ISSN 2542-193X (Online)

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Mankova A. A., Brandt N. N., Chikishev A. Y. Comparative analysis of low-frequency vibrational spectra of native and denatured proteins. Izvestiya of Saratov University. Physics , 2024, vol. 24, iss. 4, pp. 340-347. DOI: 10.18500/1817-3020-2024-24-4-340-347, EDN: BGZOZH

This is an open access article distributed under the terms of Creative Commons Attribution 4.0 International License (CC-BY 4.0).
Published online: 
25.12.2024
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Language: 
Russian
Heading: 
Optics and spectroscopy. Laser physics
Article type: 
Article
UDC: 
543.424.2
DOI: 
10.18500/1817-3020-2024-24-4-340-347
EDN: 
BGZOZH

Comparative analysis of low-frequency vibrational spectra of native and denatured proteins

Autors: 
Mankova Anna A., Lomonosov Moscow State University
Brandt Nikolay Nikolaevich, Lomonosov Moscow State University
Chikishev Andrey Yu., Lomonosov Moscow State University
Abstract: 

Background and Objectives: Changes in the secondary and tertiary structures of protein molecules during thermal denaturation lead to changes in their vibrational spectra. Vibrations corresponding to elements of the primary and secondary structure of the protein are manifested in the fingerprint range, while vibrational modes of large fragments corresponding to higher levels of the protein structural hierarchy can be observed in the low-frequency (40–500 cm−1) spectral range. The purpose of this work is to reveal changes in the vibrational spectra of proteins resulting from denaturation that can be used to characterize changes in the protein structure. Materials and Methods: Two proteins (collagen and chymotrypsin) having different secondary and tertiary structures are studied using Raman spectroscopy. The experimental data are analyzed using bandpass filtering of the Fourier transforms of the spectral curves. Results: Vibrational spectra of two proteins (collagen and chymotrypsin) having different secondary and tertiary structures, as well as the spectra of thermally denatured samples of these proteins have been measured in the fingerprint and low-frequency ranges. Several low-frequency spectral features that can be used to characterize structural changes of protein molecules have been considered. A few bands may correspond to vibrations of tertiary structure elements (both in the low-frequency range and in the “fingerprint” range). Conclusion: A comparison of the vibrational spectra of native and denatured (superhelical) collagen, as well as native and denatured (globular) chymotrypsin shows that changes in the amide I and amide III bands sensitive to the secondary structure are supplemented with spectral changes in bands that are not assigned to elements of the secondary structure and can be related to changes at higher levels of structural hierarchy. Comparison of the low-frequency vibrational spectra indicates a lower sensitivity of presumably tertiary structure of the globular protein to denaturation.

Key words: 
protein structure
secondary structure
tertiary structures
chymotrypsin
collagen
Raman spectroscopy
Acknowledgments: 
This work was supported in part by the Lomonosov Moscow State University Development Program.
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Received: 
28.06.2024
Accepted: 
30.07.2024
Published: 
25.12.2024
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