Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: implications for function and misfunction.

@article{Blanch2004RamanOA,
  title={Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: implications for function and misfunction.},
  author={Ewan W Blanch and Andrew C Gill and Alexandre G O Rhie and James Hope and Lutz Hecht and K. K. Nielsen and Laurence D. Barron},
  journal={Journal of molecular biology},
  year={2004},
  volume={343 2},
  pages={
          467-76
        }
}
The aqueous solution structure of the full-length recombinant ovine prion protein PrP(25-233), together with that of the N-terminal truncated version PrP(94-233), have been studied using vibrational Raman optical activity (ROA) and ultraviolet circular dichroism (UVCD). A sharp positive band at approximately 1315 cm(-1) characteristic of poly(L-proline) II (PPII) helix that is present in the ROA spectrum of the full-length protein is absent from that of the truncated protein, together with… CONTINUE READING

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