Journal
BIOPOLYMERS
Volume 74, Issue 1-2, Pages 163-167Publisher
WILEY
DOI: 10.1002/bip.20064
Keywords
SHaPrP(90-232); scrapie 263K; prion; transmissible spongiform encephalopathies; Syrian hamster; FTIR; dorsal root ganglia
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Fourier-transform infrared microscopic spectra of scrapie-infected nervous tissue measured at high spatial resolution (similar to6 mum) were compared with those obtained from the purified, pardly proteinase K digested scrapie isoform of the prion protein isolated from nervous tissue of hamsters infected with the same scrapie strain (263K) to elucidate similarities/dissimilarities between prion structure investigated in situ and ex vivo. A further comparison is drawn to the recombinant Syrian hamster prion protein SHaPrP(90-232) after in vitro conformational transition front the predominantly alpha-helical isoform to beta-sheet-rich structures. It is shown that prion protein structure can be investigated within tissue and that detectability of regions with elevated beta-sheet content as observed in microspectra of prion-infected tissue strongly depends on spatial resolution of the experiment. (C) 2004 Wiley Periodicals, Inc.
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