NR AXEX
AU Siemer,A.B.; Arnold,A.A.; Ritter,C.; Westfeld,T.; Ernst,M.; Riek,R.; Meier,B.H.
TI Observation of highly flexible residues in amyloid fibrils of the HET-s prion
QU Journal of the American Chemical Society 2006 Oct 11; 128(40): 13224-8
PT journal article; research support, non-u.s. gov't
AB We report the observation of undetected (until now) residues of the prion protein fragment HET-s(218-289) which give rise to well-resolved (13)C, (15)N, and (1)H 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.
MH Amino Acid Sequence; Amyloid/*chemistry; Fungal Proteins/*chemistry; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular/methods; Peptide Fragments/*chemistry; Prions/*chemistry
AD Physical Chemistry, ETH Zürich, CH-8093 Zürich, Switzerland.
SP englisch
PO USA