{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T20:29:39Z","timestamp":1791318579728,"version":"4.3.1"},"reference-count":113,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2009,1,2]],"date-time":"2009-01-02T00:00:00Z","timestamp":1230854400000},"content-version":"vor","delay-in-days":612,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2007,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Fibrillar inclusions are a characteristic feature of the neuropathology found in the \u03b1\u2010synucleinopathies such as Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Familial forms of \u03b1\u2010synucleinopathies have also been linked with missense mutations or gene multiplications that result in higher protein expression levels. In order to form these fibrils, the protein, \u03b1\u2010synuclein (\u03b1\u2010syn), must undergo a process of self\u2010assembly in which its native state is converted from a disordered conformer into a \u03b2\u2010sheet\u2010dominated form. Here, we have developed a novel polypeptide property calculator to locate and quantify relative propensities for \u03b2\u2010strand structure in the sequence of \u03b1\u2010syn. The output of the algorithm, in the form of a simple x\u2010y plot, was found to correlate very well with the location of the \u03b2\u2010sheet core in \u03b1\u2010syn fibrils. In particular, the plot features three peaks, the largest of which is completely absent for the nonfibrillogenic protein, \u03b2\u2010syn. We also report similar significant correlations for the Alzheimer's disease\u2010related proteins, A\u03b2 and tau. A substantial region of \u03b1\u2010syn is also of converting from its disordered conformation into a long amphipathic \u03b1\u2010helical protein. We have developed the aforementioned algorithm to locate and quantify the \u03b1\u2010helical hydrophobic moment in the amino acid sequence of \u03b1\u2010syn. As before, the output of the algorithm, in the form of a simple x\u2010y plot, was found to correlate very well with the location of \u03b1\u2010helical structure in membrane bilayer\u2010associated \u03b1\u2010syn.<\/jats:p>","DOI":"10.1110\/ps.062624507","type":"journal-article","created":{"date-parts":[[2007,4,24]],"date-time":"2007-04-24T14:33:30Z","timestamp":1177425210000},"page":"906-918","source":"Crossref","is-referenced-by-count":114,"title":["A simple algorithm locates \u03b2\u2010strands in the amyloid fibril core of \u03b1\u2010synuclein, A\u03b2, and tau using the amino acid sequence alone"],"prefix":"10.1002","volume":"16","author":[{"given":"Shahin","family":"Zibaee","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"O. 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