{"title":"头发的拉曼微光谱学:蛋白质二级结构的低频标记。","authors":"E I Travkina, A Yu Chikishev, N N Brandt","doi":"10.1002/jbio.202400265","DOIUrl":null,"url":null,"abstract":"<p><p>Low-frequency intervals that can be used to study the secondary structure of proteins are determined. Compared are Raman spectra of keratins from unpigmented human hair, measured in two experimental configurations: with excitation radiation coaxial with the hair and perpendicular to it. Based on the polarization sensitivity, the bands peaked at 150 and 221 cm<sup>-1</sup> are assigned to vibrations of α-helical structures. The comparison of Raman spectra of hair fragments with different contents of secondary structure elements shows that the vibrations of β-structure are manifested in a spectral interval of 270-340 cm<sup>-1</sup>. The results obtained for a particular object (hair keratin) can be used in the study of the secondary structure of proteins.</p>","PeriodicalId":94068,"journal":{"name":"Journal of biophotonics","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2024-10-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Raman Microspectroscopy of Hair: Low-Frequency Markers of Protein Secondary Structure.\",\"authors\":\"E I Travkina, A Yu Chikishev, N N Brandt\",\"doi\":\"10.1002/jbio.202400265\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Low-frequency intervals that can be used to study the secondary structure of proteins are determined. Compared are Raman spectra of keratins from unpigmented human hair, measured in two experimental configurations: with excitation radiation coaxial with the hair and perpendicular to it. Based on the polarization sensitivity, the bands peaked at 150 and 221 cm<sup>-1</sup> are assigned to vibrations of α-helical structures. The comparison of Raman spectra of hair fragments with different contents of secondary structure elements shows that the vibrations of β-structure are manifested in a spectral interval of 270-340 cm<sup>-1</sup>. The results obtained for a particular object (hair keratin) can be used in the study of the secondary structure of proteins.</p>\",\"PeriodicalId\":94068,\"journal\":{\"name\":\"Journal of biophotonics\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2024-10-13\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of biophotonics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1002/jbio.202400265\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of biophotonics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/jbio.202400265","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Raman Microspectroscopy of Hair: Low-Frequency Markers of Protein Secondary Structure.
Low-frequency intervals that can be used to study the secondary structure of proteins are determined. Compared are Raman spectra of keratins from unpigmented human hair, measured in two experimental configurations: with excitation radiation coaxial with the hair and perpendicular to it. Based on the polarization sensitivity, the bands peaked at 150 and 221 cm-1 are assigned to vibrations of α-helical structures. The comparison of Raman spectra of hair fragments with different contents of secondary structure elements shows that the vibrations of β-structure are manifested in a spectral interval of 270-340 cm-1. The results obtained for a particular object (hair keratin) can be used in the study of the secondary structure of proteins.