| Entry ID |
Data summary |
Entry Title |
Citation Title |
Authors |
| 17570 |
Chemical Shifts: 1 set
|
Solid-state NMR assignment of the C-terminal domain of the Ure2p prion in its fibrillar form |
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion.
|
Anja Bockmann, Anne Schutz, Antoine Loquet, Beat H Meier, Birgit Habenstein, Christian Wasmer, Luc Bousset, Ronald Melki, Yannick Sourigues |
| 17499 |
Chemical Shifts: 1 set
|
Solid-state NMR assignment of the Ure2p prion C-terminal 70-354 in microcrystalline form. |
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion.
|
Anja Bockmann, Anne Schutz, Antoine Loquet, Beat H Meier, Birgit Habenstein, Christian Wasmer, Luc Bousset, Ronald Melki, Yannick Sourigues |
| 16965 |
Chemical Shifts: 1 set
|
Backbone NMR assignment of the globular domain of HET-s(1-227) prion protein. |
Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227).
|
Anja Bockmann, Anne Schuetz, Beat H Meier, Birgit Habenstein, Christian Wasmer, Jason Greenwald, Rene Verel, Roland Riek |
| 16964 |
Chemical Shifts: 1 set
|
Solid-state NMR assignment of the globular domain of HET-s(1-227) prion protein in microcrystalline form. |
Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227).
|
Anja Bockmann, Anne Schuetz, Beat H Meier, Birgit Habenstein, Christian Wasmer, Jason Greenwald, Rene Verel, Roland Riek |
| 11064 |
Chemical Shifts: 1 set
|
Solid-state NMR assignment of the rigid core of the HET-s(218-289) prion protein in its amyloid conformation. |
A Combined Solid-State NMR and MD Characterization of the Stability and Dynamics of the HET-s(218-289) Prion in its Amyloid Conformation
|
Adam Lange, Alice Soragni, Beat H Meier, Christian Wasmer, Helene Van Melckebeke, Wilfred F Van Gunsteren, Zrinka Gattin |
| 11028 |
Chemical Shifts: 1 set
|
Solid-state NMR assignment of the rigid core of the HET-s(218-289) prion protein in its amyloid conformation. |
Amyloid fibrils of the HET-s(218-289) prion form a beta-solenoid with a triangular hydrophobic core.
|
Adam Lange, Ansgar Siemer, Beat H Meier, Christian Wasmer, Helene Van Melckebeke, Roland Riek |
