THE STUDY OF TURNIP MOSAIC-VIRUS COAT PROTEIN BY SURFACE-ENHANCED RAMAN-SPECTROSCOPY

Using Turnip Mosaic virus (TuMV) coat protein as material, the seconda ry structure has been studied by both normal Raman spectroscopy (NRS) and surface enhanced Raman spectroscopy (SERS). The NRS of TuMV coat p rotein under certain conditions showed the alpha-helix, beta-sheet and random coil structure. The C-S-S-C comformations are trans-gauche-gau che and gauche-gauche-gauche. The SERS spectrum of TuMV coat protein u nder certain conditions reveals the alpha-helix structure. By studying SERS at different adsorbing times, we have observed the amide III vib ration of alpha-helix, beta-sheet and random coil structure. The C-S-S -C conformations drawn from the SERS spectra are trans-gauche-gauche a nd trans-gauche-trans. Besides the amide I, amide III and C-S-S-C band s, the Calpha-C-N band, aromatic amino acid bands and some other bands can also be seen in the SERS spectra.