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Solid-State NMR Studies of the Fibril Forming Protein PABPN1

✍ Scribed by Huster, Daniel; Scheidt, Holger A.; Lodderstedt, Grit; Schwarz, Elisabeth

Book ID
119204888
Publisher
Biophysical Society
Year
2009
Tongue
English
Weight
40 KB
Volume
96
Category
Article
ISSN
0006-3495

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## Abstract Conformational changes in the prion protein (PrP) seem to be responsible for prion diseases. We have used conformation‐dependent chemical‐shift measurements and rotational‐resonance distance measurements to analyze the conformation of solid‐state peptides lacking long‐range order, corre