NMR structure of the mouse prion protein domain PrP(121–231)

2021 ◽  
pp. 117-119
Author(s):  
Roland Riek ◽  
Simone Hornemann ◽  
Gerhard Wider ◽  
Martin Billeter ◽  
Rudi Glockshuber ◽  
...  
Keyword(s):  
Prion Protein ◽  
Nmr Structure ◽  
Protein Domain

NMR structure of the mouse prion protein domain PrP(121–231)

Nature ◽  
1996 ◽  
Vol 382 (6587) ◽  
pp. 180-182 ◽  
Author(s):  
Roland Riek ◽  
Simone Hornemann ◽  
Gerhard Wider ◽  
Martin Billeter ◽  
Rudi Glockshuber ◽  
...  
Keyword(s):  
Prion Protein ◽  
Nmr Structure ◽  
Protein Domain

scholarly journals NMR Structure of the Bank Vole Prion Protein at 20 °C Contains a Structured Loop of Residues 165–171

2008 ◽  
Vol 383 (2) ◽  
pp. 306-312 ◽  
Author(s):  
Barbara Christen ◽  
Daniel R. Pérez ◽  
Simone Hornemann ◽  
Kurt Wüthrich
Keyword(s):  
Prion Protein ◽  
Bank Vole ◽  
Nmr Structure

scholarly journals NMR structure of the bovine prion protein

2000 ◽  
Vol 97 (15) ◽  
pp. 8334-8339 ◽  
Author(s):  
F. Lopez Garcia ◽  
R. Zahn ◽  
R. Riek ◽  
K. Wuthrich
Keyword(s):  
Prion Protein ◽  
Nmr Structure

scholarly journals NMR Structure and CD Titration with Metal Cations of Human Prionα2-Helix-Related Peptides

2007 ◽  
Vol 2007 ◽  
pp. 1-9 ◽  
Author(s):  
Luisa Ronga ◽  
Pasquale Palladino ◽  
Gabriella Saviano ◽  
Teodorico Tancredi ◽  
Ettore Benedetti ◽  
...  
Keyword(s):  
Prion Protein ◽  
Point Mutations ◽  
Metal Cations ◽  
Spectroscopic Studies ◽  
Cation Binding ◽  
Protein Domain ◽  
Wild Type ◽  
Peptide Complexes ◽  
Natural Target

The 173–195 segment corresponding to the helix 2 of the C-globular prion protein domain could be one of several “spots” of intrinsic conformational flexibility. In fact, it possesses chameleon conformational behaviour and gathers several disease-associated point mutations. We have performed spectroscopic studies on the wild-type fragment 173–195 and on its D178N mutant dissolved in trifluoroethanol to mimic the in vivo system, both in the presence and in the absence of metal cations. NMR data showed that the structure of the D178N mutant is characterized by two short helices separated by a kink, whereas the wild-type peptide is fully helical. Both peptides retained these structural organizations, as monitored by CD, in the presence of metal cations. NMR spectra were however not in favour of the formation of definite ion-peptide complexes. This agrees with previous evidence that other regions of the prion protein are likely the natural target of metal cation binding.

NMR Structure of a Variant Human Prion Protein with Two Disulfide Bridges

2003 ◽  
Vol 326 (1) ◽  
pp. 225-234 ◽  
Author(s):  
Ralph Zahn ◽  
Peter Güntert ◽  
Christine von Schroetter ◽  
Kurt Wüthrich
Keyword(s):  
Prion Protein ◽  
Nmr Structure ◽  
Disulfide Bridges ◽  
Human Prion Protein

Three-dimensional NMR structure of a self-folding domain of the prion protein PrP(121–231)

1997 ◽  
Vol 22 (7) ◽  
pp. 241-242 ◽  
Author(s):  
Rudi Glockshuber ◽  
Simone Hornemann ◽  
Roland Riek ◽  
Gerhard Wider ◽  
Martin Billeter ◽  
...  
Keyword(s):  
Prion Protein ◽  
Three Dimensional ◽  
Nmr Structure

scholarly journals NMR Structure of the Human Prion Protein with the Pathological Q212P Mutation Reveals Unique Structural Features

PLoS ONE ◽  
2010 ◽  
Vol 5 (7) ◽  
pp. e11715 ◽  
Author(s):  
Gregor Ilc ◽  
Gabriele Giachin ◽  
Mariusz Jaremko ◽  
Łukasz Jaremko ◽  
Federico Benetti ◽  
...  
Keyword(s):  
Prion Protein ◽  
Structural Features ◽  
Nmr Structure ◽  
Human Prion Protein
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