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NMR processing:
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Side-chains:
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
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Fragment-based:
BMRB CS-Rosetta
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Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
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Torsion angles from chemical shifts:
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TALOS
Promega- Proline
Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Methyl S2
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From structure:
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ArShift- Aromatic
ShiftS
Proshift
PPM
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From sequence:
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Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
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Default NMR structure of the mouse prion protein domain PrP(121-321).

NMR structure of the mouse prion protein domain PrP(121-321).

Related Articles NMR structure of the mouse prion protein domain PrP(121-321).

Nature. 1996 Jul 11;382(6587):180-2

Authors: Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wüthrich K

The 'protein only' hypothesis states that a modified form of normal prion protein triggers infectious neurodegenerative diseases, such as bovine spongiform encephalopathy (BSE), or Creutzfeldt-Jakob disease (CJD) in humans. Prion proteins are thought to exist in two different conformations: the 'benign' PrPcform, and the infectious 'scrapie form', PrPsc. Knowledge of the three-dimensional structure of PrPc is essential for understanding the transition to PrPsc. The nuclear magnetic resonance (NMR) structure of the autonomously folding PrP domain comprising residues 121-231 (ref. 6) contains a two-stranded antiparallel beta-sheet and three alpha-helices. This domain contains most of the point-mutation sites that have been linked, in human PrP, to the occurrence of familial prion diseases. The NMR structure shows that these mutations occur within, or directly adjacent to, regular secondary structures. The presence of a beta-sheet in PrP(121-231) is in contrast with model predictions of an all-helical structure of PrPc (ref. 8), and may be important for the initiation of the transition from PrPc to PrPsc.

PMID: 8700211 [PubMed - indexed for MEDLINE]



Source: PubMed
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