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首页> 外文期刊>Optics and Spectroscopy >A Spectroscopic Study of Changes in the Secondary Structure of Proteins of Biological Fluids of the Oral Cavity by Synchrotron Infrared Microscopy
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A Spectroscopic Study of Changes in the Secondary Structure of Proteins of Biological Fluids of the Oral Cavity by Synchrotron Infrared Microscopy

机译:Syschrotron红外显微镜通过Synchrotron红外显微镜的蛋白质蛋白质二次结构变化的光谱研究

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摘要

On the basis of the data of infrared spectroscopy with synchrotron radiation, the secondary structure of proteins of the dentinal and gingival fluids during the development of cariosity in deep dentin tissues is studied. It is shown that the change in the shape of the profile of the amide I band in the region of 1700-1605 cm(-1) is associated both with a change in the ratio of the integrated absorption intensities of the alpha-helix and beta-sheet secondary structures and with the position of the beta-coil and beta-sheet components in the spectrum. It is established that the alpha-helix/beta-sheet ratio for both dentinal and gingival fluids is below the threshold level, at which significant changes in the secondary structure of proteins of biological fluids are observed, unequivocally indicating the development of pathology in hard dental tissues. The features that we discovered in the profile of the amide I band of biological fluids of the oral cavity, together with the spectral markers of the development of cariosity in dentin, are reliable spectroscopic signatures of the pathology and can be detected using the gingival fluid.
机译:基于具有同步辐射的红外光谱学的数据,研究了在深牙本组织中躁动性发育过程中牙本质和牙龈液的蛋白质的二次结构。结果表明,在1700-1605cm(-1)区域中的酰胺I带的轮廓的形状的变化与α-螺旋和β的集成吸收强度的比率的变化有关 - 次级结构和β-线圈和β-薄板组分的位置。建立牙本质和牙龈液的α-螺旋/β-板材比率低于阈值水平,在该阈值水平下,观察到生物流体蛋白二次结构的显着变化,明确表明在硬牙齿中的病理学的发展组织。我们在口腔的生物流体的酰胺I带的轮廓中发现的特征,以及牙本质中躁动性的发育的光谱标记,是病理学的可靠光谱签名,并且可以使用牙龈液检测。

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