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J. Am. Chem. Soc. In Journal of the American Chemical Society, Vol. 128, No. 40. (15 September 2006), pp. 13224-13228, doi:10.1021/ja063639x Key: citeulike:12181205
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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 by measuring the lateral diffusion constants. The amino acids identified in the spectra are compatible with their localization in the segments of the protein which could not be detected in earlier solid-state NMR experiments. 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 suggest that they belong to different parts of the same molecule.
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