{"title":"通过傅立叶变换红外差分光谱法研究暴露于频率为 8-18 GHz 的微波中的膜蛋白 Bacteriorhodopsin 的二级结构","authors":"E. L. Terpugov, O. V. Degtyareva, E. E. Fesenko","doi":"10.1134/S0006350924700921","DOIUrl":null,"url":null,"abstract":"<div><p>Fourier transform infrared difference spectroscopy was used to study the effect of millimeter-range electromagnetic radiation on the structure of bacteriorhodopsin under lighting conditions. A detailed analysis of the Fourier IR spectra revealed pronounced structural changes in the region of amide I, amide II and rearrangement of the hydrogen bond network. The well-resolved peaks of the amide bands made it possible to recognize two different components (α-I and α-II) of the α-helical conformation of the opsin. Irreversible conformational changes of bacteriorhodopsin in purple membranes detected by Fourier IR difference spectroscopy suggested that microwaves induced structural rearrangements of proteins unrelated to temperature.</p></div>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"69 5","pages":"836 - 845"},"PeriodicalIF":4.0330,"publicationDate":"2025-03-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The Study of the Secondary Structure of a Membrane Protein Bacteriorhodopsin Exposed to Microwaves with a Frequency of 8–18 GHz by Fourier Transform IR Difference Spectroscopy\",\"authors\":\"E. L. Terpugov, O. V. Degtyareva, E. E. Fesenko\",\"doi\":\"10.1134/S0006350924700921\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Fourier transform infrared difference spectroscopy was used to study the effect of millimeter-range electromagnetic radiation on the structure of bacteriorhodopsin under lighting conditions. A detailed analysis of the Fourier IR spectra revealed pronounced structural changes in the region of amide I, amide II and rearrangement of the hydrogen bond network. The well-resolved peaks of the amide bands made it possible to recognize two different components (α-I and α-II) of the α-helical conformation of the opsin. Irreversible conformational changes of bacteriorhodopsin in purple membranes detected by Fourier IR difference spectroscopy suggested that microwaves induced structural rearrangements of proteins unrelated to temperature.</p></div>\",\"PeriodicalId\":493,\"journal\":{\"name\":\"Biophysics\",\"volume\":\"69 5\",\"pages\":\"836 - 845\"},\"PeriodicalIF\":4.0330,\"publicationDate\":\"2025-03-06\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biophysics\",\"FirstCategoryId\":\"4\",\"ListUrlMain\":\"https://link.springer.com/article/10.1134/S0006350924700921\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"Biochemistry, Genetics and Molecular Biology\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biophysics","FirstCategoryId":"4","ListUrlMain":"https://link.springer.com/article/10.1134/S0006350924700921","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 0
摘要
利用傅立叶变换红外差分光谱法研究了在光照条件下毫米范围电磁辐射对细菌视紫红质结构的影响。对傅立叶红外光谱的详细分析显示,酰胺 I、酰胺 II 和氢键网络重排区域的结构发生了明显变化。由于酰胺带的峰值分辨良好,因此可以识别出α螺旋构象的两种不同成分(α-I 和 α-II)。傅立叶红外差分光谱法检测到紫色膜中细菌眼色素的不可逆构象变化,这表明微波诱导蛋白质的结构重排与温度无关。
The Study of the Secondary Structure of a Membrane Protein Bacteriorhodopsin Exposed to Microwaves with a Frequency of 8–18 GHz by Fourier Transform IR Difference Spectroscopy
Fourier transform infrared difference spectroscopy was used to study the effect of millimeter-range electromagnetic radiation on the structure of bacteriorhodopsin under lighting conditions. A detailed analysis of the Fourier IR spectra revealed pronounced structural changes in the region of amide I, amide II and rearrangement of the hydrogen bond network. The well-resolved peaks of the amide bands made it possible to recognize two different components (α-I and α-II) of the α-helical conformation of the opsin. Irreversible conformational changes of bacteriorhodopsin in purple membranes detected by Fourier IR difference spectroscopy suggested that microwaves induced structural rearrangements of proteins unrelated to temperature.
BiophysicsBiochemistry, Genetics and Molecular Biology-Biophysics
CiteScore
1.20
自引率
0.00%
发文量
67
期刊介绍:
Biophysics is a multidisciplinary international peer reviewed journal that covers a wide scope of problems related to the main physical mechanisms of processes taking place at different organization levels in biosystems. It includes structure and dynamics of macromolecules, cells and tissues; the influence of environment; energy transformation and transfer; thermodynamics; biological motility; population dynamics and cell differentiation modeling; biomechanics and tissue rheology; nonlinear phenomena, mathematical and cybernetics modeling of complex systems; and computational biology. The journal publishes short communications devoted and review articles.