The study of Turnip Mosaic virus coat protein by surface enhanced Raman spectroscopy

Using Turnip Mosaic virus (TuMV) coat protein as material, the secondary structure has been studied by both normal Raman spectroscopy (NRS) and surface enhanced Raman spectroscopy (SERS). The NRS of TuMV coat protein under certain conditions showed the α-helix, β-sheet and random coil structure. The...

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Bibliographic Details
Published in:Spectrochimica acta. Part A: Molecular spectroscopy 1993-11, Vol.49 (12), p.1709-1714
Main Authors: Deng, Hongying, He, Qizhi, Xu, Zhisan, Wang, Xiaohua, Sheng, Rongsheng
Format: Article
Language:English
Subjects:
Agronomy. Soil science and plant productions
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Microbiology
Morphology, structure, chemical composition, physicochemical properties
Virology
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Summary:Using Turnip Mosaic virus (TuMV) coat protein as material, the secondary structure has been studied by both normal Raman spectroscopy (NRS) and surface enhanced Raman spectroscopy (SERS). The NRS of TuMV coat protein under certain conditions showed the α-helix, β-sheet and random coil structure. The CSSC comformations are trans—gauche—gauche and gauche—gauche—gauche. The SERS spectrum of TuMV coat protein under certain conditions reveals the α-helix structure. By studying SERS at different adsorbing times, we have observed the amide III vibration of α-helix, β-sheet and random coil structure. The CSSC conformations drawn from the SERS spectra are trans—gauche—gauche and trans—gauche—trans. Besides the amide I, amide III and CSSC bands, the CαCN band, aromatic amino acid bands and some other bands can also be seen in the SERS spectra.
ISSN:0584-8539
DOI:10.1016/0584-8539(93)80238-6