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  • Title: A comparison of the solution structures of tobacco rattle and tobacco mosaic viruses from Raman optical activity.
    Author: Blanch EW, Robinson DJ, Hecht L, Barron LD.
    Journal: J Gen Virol; 2001 Jun; 82(Pt 6):1499-1502. PubMed ID: 11369896.
    Abstract:
    Vibrational Raman optical activity (ROA) spectra of tobacco rattle virus (TRV) and tobacco mosaic virus (TMV) were measured and compared with a view to obtaining new information about the coat protein subunit structure of TRV. A sharp strong positive band observed at approximately 1344 cm(-1) in the ROA spectra of the two viruses is evidence that both contain a significant amount of a hydrated form of alpha-helix, but more in TRV than in TMV. Although the ROA spectrum of TMV shows significant positive intensity in the range approximately 1297-1312 cm(-1) characteristic of alpha-helix in a hydrophobic environment, as expected from the helix interface residues in the four-helix bundles that constitute the basic motif of the TMV coat protein fold, that of TRV shows little positive ROA intensity here. Instead TRV shows a strong positive ROA band at approximately 1315 cm(-1), of much greater intensity than bands shown here by TMV, that is characteristic of polyproline II (PPII) helix. This suggests that the additional long central and C-terminal sequences of the TRV coat proteins contain a significant amount of PPII structure, plus perhaps some beta-strand judging by a prominent sharp negative ROA band shown by TRV at approximately 1236 cm(-1), but little alpha-helix. The open flexible hydrated nature of PPII helical structure is consistent with the earlier suggestions that the additional sequences are exposed and, together with a larger amount of hydrated alpha-helix, could serve to fill the extra volume required by the larger diameter of the cylindrical TRV particles relative to those of TMV.
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