@article {300,
	title = {Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP89-143(P101L)},
	journal = {Solid State Nuclear Magnetic Resonance},
	volume = {29},
	year = {2006},
	note = {Solid State Nucl Mag999VATimes Cited:22Cited References Count:34},
	month = {Feb},
	pages = {183-190},
	abstract = {<p>The peptide fragment 89-143 of the prion protein (carrying a P101L mutation) is biologically active in transgenic mice when in a fibrillar form. Injection of these fibrils into transgenic mice (expressing full length PrP with the P101L mutation) induces a neurodegenerative prion disease (Kaneko et al., J. Mol. Biol. 295 (2000) 997). Here we present solid-state NMR studies of PrP89-143(P101L) fibrils, probing the conformation of residues in the hydrophobic segment 112-124 with chemical shifts. The conformations of glycine residues were analyzed using doubly C-13 = 0 labeled peptides by two-dimensional (2D) double-quantum correlation, and double-quantum filtered dephasing distance measurements. MQ-NMR experiments were carried out to probe the relative alignment of the individual peptides fibrils. These NMR studies indicate that the 112-124 segment adopts an extended beta-sheet conformation, though not in a parallel, in register alignment. There is evidence for conformational variability at Gly 113. DQ correlation experiments provide useful information in regions with conformational heterogeneity. (c) 2005 Elsevier Inc. All rights reserved.</p>
},
	keywords = {identification},
	isbn = {0926-2040},
	doi = {Doi 10.1016/J.Ssnmr.2005.09.017},
	url = {<Go to ISI>://WOS:000234417500020},
	author = {Lim, K. H. and Nguyen, T. N. and Damo, S. M. and Mazur, T. and Ball, H. L. and Prusiner, S. B. and Pines, A. and Wemmer, D. E.}
}
