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

Blanch, Ewan W., Gill, Andrew C., Rhie, Alexandre G. O., Hope, James ORCID: https://orcid.org/0000-0003-2015-2389, Hecht, Lutz, Nielsen, Kurt and Barron, Laurence D. (2004) Raman optical activity demonstrates poly(l-proline) II helix in the N-terminal region of the ovine prion protein:Implications for function and misfunction. Journal of Molecular Biology, 343 (2). pp. 467-476. ISSN 0022-2836

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Abstract

The aqueous solution structure of the full-length recombinant ovine prion protein PrP25-233, together with that of the N-terminal truncated version PrP94-233, have been studied using vibrational Raman optical activity (ROA) and ultraviolet circular dichroism (UVCD). A sharp positive band at ∼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 bands characteristic of β-turns. Although it is not possible similarly to identify PPII helix in the full-length protein directly from its UVCD spectrum, subtraction of the UVCD spectrum of PrP94-233 from that of PrP25-233 yields a difference UVCD spectrum also characteristic of PPII structure and very similar to the UVCD spectrum of murine PrP25-113. These results provide confirmation that a major conformational element in the N-terminal region is PPII helix, but in addition show that the PPII structure is interspersed with β-turns and that little PPII structure is present in PrP94-233. A principal component analysis of the ROA data indicates that the α-helix and β-sheet content, located in the structured C-terminal domain, of the full-length and truncated proteins are similar. The flexibility imparted by the high PPII content of the N-terminal domain region may be an essential factor in the function and possibly also the misfunction of prion proteins.

Item Type:	Article
Uncontrolled Keywords:	amyloid fibrils,ovine prion protein,poly(l-proline) ii helix,raman optical activity,transmissible spongiform encephalopathy,structural biology,molecular biology ,/dk/atira/pure/subjectarea/asjc/1300/1315
Faculty \ School:	Faculty of Science > School of Biological Sciences
Related URLs:	https://www.scopus.com/pages/publication...
Depositing User:	LivePure Connector
Date Deposited:	05 Dec 2025 13:30
Last Modified:	18 Jun 2026 20:49
URI:	https://ueaeprints.uea.ac.uk/id/eprint/101294
DOI:	10.1016/j.jmb.2004.08.058

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