{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T02:28:15Z","timestamp":1790994495838,"version":"4.1.0"},"reference-count":42,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":5509,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1993,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The scrapie amyloid (prion) protein (PrP27\u201330) is the protease\u2010resistant core of a larger precursor (PrP<jats:sup>Sc<\/jats:sup>) and a component of the infectious scrapie agent; the potential to form amyloid is a result of a posttranslational event or conformational abnormality. The conformation, heat stability, and solvent\u2010induced conformational transitions of PrP27\u201330 were studied in the solid state in films by CD spectroscopy and correlated with the infectivity of rehydrated and equilibrated films. The exposure of PrP27\u201330 in films to 60 \u00b0C, 100 \u00b0C, and 132 \u00b0C for 30 min did not change the <jats:italic>\u03b2<\/jats:italic>\u2010sheet secondary structure; the infectivity slightly diminished at 132 \u00b0C and correlated with a decreased solubility of PrP27\u201330 in sodium dodecyl sulfate (SDS), probably due to cross\u2010linking. Exposing PrP27\u201330 films to formic acid (FA), trifluoroacetic acid (TFA), trifluoroethanol (TFE), hexafluoro\u20102\u2010propanol (HFIP), and SDS transformed the amide CD band, diminished the mean residue ellipticity of aromatic bands, and inactivated scrapie infectivity. The convex constraint algorithm (CAA) deconvolution of the CD spectra of the solvent\u2010exposed and rehydrated solid state PrP27\u201330 identified five common spectral components. The loss of infectivity quantitatively correlated with a decreasing proportion of native, <jats:italic>\u03b2<\/jats:italic>\u2010pleated sheet\u2010like secondary structure component, an increasing amount of <jats:italic>\u03b1<\/jats:italic>\u2010helical component, and an increasingly disordered tertiary structure. The results demonstrate the unusual thermal stability of the <jats:italic>\u03b2<\/jats:italic>\u2010sheet secondary structure of PrP27\u201330 protein in the solid state. The conformational perturbations of PrP27\u201330 parallel the changes in infectivity and suggest that the <jats:italic>\u03b2<\/jats:italic>\u2010sheet structure plays a key role in the physical stability of scrapie amyloid and in the ability to propagate and replicate scrapie.<\/jats:p>","DOI":"10.1002\/pro.5560021220","type":"journal-article","created":{"date-parts":[[2009,2,10]],"date-time":"2009-02-10T00:20:35Z","timestamp":1234225235000},"page":"2206-2216","source":"Crossref","is-referenced-by-count":173,"title":["Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity"],"prefix":"10.1002","volume":"2","author":[{"given":"Jiri","family":"Safar","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter P.","family":"Roller","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D. 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