Dynamics of a truncated prion protein, PrP(113-231), from (15)N NMR relaxation: order parameters calculated and slow conformational fluctuations localized to a distinct region.

ABSTRACT: Prion diseases are associated with the misfolding of the prion protein (PrP(C)) from a largely alpha-helical isoform to a beta-sheet rich oligomer (PrP(Sc)). Flexibility of the polypeptide could contribute to the ability of PrP(C) to undergo the conformational rearrangement during PrP(C)-PrP(Sc) interactions, which then leads to the misfolded isoform. We have therefore examined the molecular motions of mouse PrP(C), residues 113-231, in solution, using (15)N NMR relaxation measurements. A truncated fragment has been used to eliminate the effect of the 90-residue unstructured tail of PrP(C) so the dynamics of the structured domain can be studied in isolation. (15)N longitudinal (T(1)) and transverse relaxation (T(2)) times as well as the proton-nitrogen nuclear Overhauser effects have been

SUBMITTER: O'Sullivan DB 

PROVIDER: S-EPMC2708060 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature