The study of Turnip Mosaic virus coat protein by surface enhanced Raman spectroscopy |
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| Institution: | 1. Institute of Medicinal and Pharmaceutical Chemistry, TU Braunschweig, D-38106 Braunschweig, Germany;2. Chemistry Department, Faculty of Science, King Abdulaziz University, 80203 Jeddah, Saudi Arabia;3. Chemistry Department, Faculty of Science, University of Jeddah, Jeddah, Saudi Arabia;4. Chemistry Department, Faculty of Science, Assiut University, 71516 Assiut, Egypt |
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| Abstract: | 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 CSSC 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 CSSC conformations drawn from the SERS spectra are trans—gauche—gauche and trans—gauche—trans. Besides the amide I, amide III and CSSC bands, the CαCN band, aromatic amino acid bands and some other bands can also be seen in the SERS spectra. |
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