Observation of Highly Flexible Residues in Amyloid Fibrils of the HET-s Prion

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• 作者：Ansgar B. Siemer ; Alexandre A. Arnold ; Christiane Ritter ; Thomas Westfeld ; Matthias Ernst ; Roland Riek ; Beat H. Meier
• 刊名：Journal of the American Chemical Society
• 出版年：2006
• 出版时间：October 11, 2006
• 年：2006
• 卷：128
• 期：40
• 页码：13224 - 13228
• 全文大小：384K
• 年卷期：v.128,no.40(October 11, 2006)
• ISSN：1520-5126

文摘

We report the observation of undetected (until now) residues of the prion protein fragment HET-s(218-289) which give rise to well-resolved ¹³C, ¹⁵N, and ¹H NMR resonances under high-resolution magic-angle spinning (HRMAS) conditions. The observed signals belong to large polymeric units as shown bymeasuring the lateral diffusion constants. The amino acids identified in the spectra are compatible withtheir localization in the segments of the protein which could not be detected in earlier solid-state NMRexperiments. The observed chemical shifts indicate that these residues are in a random-coil conformation.Complementary experiments which detect only dynamic or static residues, respectively, strongly suggestthat they belong to different parts of the same molecule.