Major prion protein
UniProt P04156 · gene PRNP · Homo sapiens · 253 residues
121evidence items
0mapped to a state
0states
8techniques
6sources
0conflicts
Coverage grid
Mapped evidence per state and technique. Shaded rows rest on a single technique. Badge = best data level in the cell: raw (traces, images, FIDs: can be re-analysed), proc (maps, curves, tables, trajectories) or rep (values in the paper only).
| State | Basis | xray | cryoem | microed | nmr_structure | nmr_shifts | saxs_sans | force_spectroscopy | af_prediction | Total |
|---|---|---|---|---|---|---|---|---|---|---|
| No states defined yet. | ||||||||||
Unmapped evidence: 121 of 121 items. Mappings come from curator assignments and curated rules; see About for how rules work.
Sources
| Source | Evidence | Mapped |
|---|---|---|
| AlphaFold DB | 1 | 0 |
| BMRB | 25 | 0 |
| DisProt | 2 | 0 |
| RCSB PDB | 72 | 0 |
| SASBDB | 4 | 0 |
| SMASH-BIO | 17 | 0 |
Structure
No state models are exported for this protein yet. Observed states export the representative PDB entry; inferred states need fitted models, not yet built.
States and transitions
No states defined.
| State | Basis | Parent | Description |
|---|
No transitions recorded in this version (no rate or free-energy evidence has been curated yet).
Evidence
One row per deposit or experiment. Filter by technique, environment or text. Unmapped evidence is listed too.
| Evidence | Technique | Observable | Conditions | Mapped to state |
|---|---|---|---|---|
| EV-PDB-1QM2-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein fragment 121-230 · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-4N9O-1 RCSB PDB | xray | resolution: 1.5 Å | in vitro · -173.15 °C · pH 7 Probing the N-terminal beta-sheet conversion in the crystal structure of the human prion protein bound to a Nanobody · Major prion protein (chains A) | unmapped |
| EV-PDB-4KML-1 RCSB PDB | xray | resolution: 1.5 Å | in vitro · -73.15 °C · pH 6 Probing the N-terminal beta-sheet conversion in the crystal structure of the full-length human prion protein bound to a Nanobody · Major prion protein (chains A) | unmapped |
| EV-PDB-4E1I-2 RCSB PDB | xray | resolution: 2.03 Å | in vitro · -173.15 °C · pH 5.5 Fragment of human prion protein · Major prion protein (chains B,D,F,H,J,L) | unmapped |
| EV-PDB-4E1I-1 RCSB PDB | xray | resolution: 2.03 Å | in vitro · -173.15 °C · pH 5.5 Fragment of human prion protein · Major prion protein (chains A,C,E,G,I,K) | unmapped |
| EV-PDB-4E1H-2 RCSB PDB | xray | resolution: 1.4 Å | in vitro · -173.15 °C · pH 3.5 · ligands CIT, FE Fragment of human prion protein · Major prion protein (chains B,D,F,H,J,L) | unmapped |
| EV-PDB-4E1H-1 RCSB PDB | xray | resolution: 1.4 Å | in vitro · -173.15 °C · pH 3.5 · ligands CIT, FE Fragment of human prion protein · Major prion protein (chains A,C,E,G,I,K) | unmapped |
| EV-PDB-4DGI-1 RCSB PDB | xray | resolution: 2.4 Å | in vitro · -173.15 °C · pH 6.5 · ligands NA Structure of POM1 FAB fragment complexed with human PrPc Fragment 120-230 · Major prion protein (chains A) | unmapped |
| EV-PDB-3NVF-1 RCSB PDB | xray | resolution: 1.8 Å | in vitro · -173.15 °C · pH 7.4 · ligands MPD IIHFGS segment 138-143 from human prion · Major prion protein (chains A) | unmapped |
| EV-PDB-3NHD-1 RCSB PDB | xray | resolution: 1.92 Å | in vitro · -173.15 °C · pH 5.5 · ligands ACY GYVLGS segment 127-132 from human prion with V129 · Major prion protein (chains A,B) | unmapped |
| EV-PDB-3NHC-1 RCSB PDB | xray | resolution: 1.57 Å | in vitro · -173.15 °C · pH 7 GYMLGS segment 127-132 from human prion with M129 · Major prion protein (chains A,B) | unmapped |
| EV-PDB-3MD5-1 RCSB PDB | xray | resolution: 1.4 Å | in vitro · -173.15 °C · pH 6.5 Prion peptide · Major prion protein (chains A,B) | unmapped |
| EV-PDB-3MD4-1 RCSB PDB | xray | resolution: 1.15 Å | in vitro · -173.15 °C · pH 7.5 Prion peptide · Major prion protein (chains A,B) | unmapped |
| EV-PDB-3HJX-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C · pH 7 · ligands CD, CL Human prion protein variant D178N with V129 · Major prion protein (chains A) | unmapped |
| EV-PDB-3HJ5-1 RCSB PDB | xray | resolution: 3.1 Å | in vitro · -173.15 °C · pH 8 Human prion protein variant V129 domain swapped dimer · Major prion protein (chains A,B) | unmapped |
| EV-PDB-3HES-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C · pH 8.5 · ligands CD Human prion protein variant F198S with M129 · Major prion protein (chains A,B) | unmapped |
| EV-PDB-3HER-1 RCSB PDB | xray | resolution: 1.85 Å | in vitro · -173.15 °C · pH 8.5 · ligands CD Human prion protein variant F198S with V129 · Major prion protein (chains A,B) | unmapped |
| EV-PDB-3HEQ-1 RCSB PDB | xray | resolution: 1.8 Å | in vitro · -173.15 °C · pH 8 · ligands CD Human prion protein variant D178N with M129 · Major prion protein (chains A,B) | unmapped |
| EV-PDB-3HAK-1 RCSB PDB | xray | resolution: 1.8 Å | in vitro · -173.15 °C · pH 5.2 Human prion protein variant V129 · Major prion protein (chains A) | unmapped |
| EV-PDB-3HAF-1 RCSB PDB | xray | resolution: 2.26 Å | in vitro · -173.15 °C · pH 10 · ligands CD, CL Human prion protein variant V129 domain swapped dimer · Major prion protein (chains A) | unmapped |
| EV-PDB-2W9E-1 RCSB PDB | xray | resolution: 2.9 Å | in vitro · -173.15 °C · pH 8 · ligands SO4 Structure of ICSM 18 (anti-Prp therapeutic antibody) Fab fragment complexed with human Prp fragment 119-231 · MAJOR PRION PROTEIN (chains A) | unmapped |
| EV-PDB-2OL9-1 RCSB PDB | xray | resolution: 0.85 Å | in vitro · -173.15 °C · pH 7 Peptide corresponding to residues 170-175 of human prion · peptide from human prion (chains A) | unmapped |
| EV-PDB-2M8T-1 RCSB PDB | nmr_structure | structure | in vitro · 25.85 °C · pH 4.6 Solution NMR structure of the V209M variant of the human prion protein (residues 90-231) · Major prion protein (chains A) | unmapped |
| EV-PDB-2LV1-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 7.2 Solution-state NMR structure of prion protein mutant V210I at neutral pH · Major prion protein (chains A) | unmapped |
| EV-PDB-2LSB-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 5.5 Solution-state NMR structure of the human prion protein · Major prion protein (chains A) | unmapped |
| EV-PDB-2LFT-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 5.5 Human prion protein with E219K protective polymorphism · Major prion protein (chains A) | unmapped |
| EV-PDB-2LEJ-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 5.5 human prion protein mutant HuPrP(90-231, M129, V210I) · Major prion protein (chains A) | unmapped |
| EV-PDB-2LBG-1 RCSB PDB | nmr_structure | structure | in vitro · 36.85 °C · pH 7.6 Structure of the CHR of the Prion protein in DPC Micelles · Major prion protein (chains A) | unmapped |
| EV-PDB-2KUN-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 5.5 Three dimensional structure of HuPrP(90-231 M129 Q212P) · Major prion protein (chains A) | unmapped |
| EV-PDB-2K1D-1 RCSB PDB | nmr_structure | structure | in vitro · 25.85 °C · pH 4.6 NMR Studies of a Pathogenic Mutant (D178N) of the Human Prion Protein · Major prion protein (chains A) | unmapped |
| EV-PDB-2IV6-1 RCSB PDB | nmr_structure | structure | in vitro · 26.85 °C · pH 5 hPrP-173-195-D178N solution structure · MAJOR PRION PROTEIN (chains A) | unmapped |
| EV-PDB-2IV5-1 RCSB PDB | nmr_structure | structure | in vitro · 26.85 °C · pH 5 hPrP-173-195 solution structure · MAJOR PRION PROTEIN (chains A) | unmapped |
| EV-PDB-2IV4-1 RCSB PDB | nmr_structure | structure | in vitro · 26.85 °C · pH 5 hPrP180-195 structure · MAJOR PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1QM3-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein fragment 121-230 · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1QM1-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein fragment 90-230 · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1QM0-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein fragment 90-230 · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1QLZ-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1QLX-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1OEI-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein 61-84 · MAJOR PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1OEH-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein 61-68 · MAJOR PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1I4M-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C · pH 8 · ligands CD, CL Crystal structure of the human prion protein reveals a mechanism for oligomerization · MAJOR PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1HJN-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 7 HUMAN PRION PROTEIN AT PH 7.0 · MAJOR PRION PROTEIN PRECURSOR (chains A) | unmapped |
| EV-PDB-1HJM-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 7 HUMAN PRION PROTEIN AT PH 7.0 · MAJOR PRION PROTEIN PRECURSOR (chains A) | unmapped |
| EV-PDB-1H0L-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 HUMAN PRION PROTEIN 121-230 M166C/E221C · MAJOR PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1FO7-1 RCSB PDB | nmr_structure | structure | in vitro · 25.85 °C · pH 4.6 HUMAN PRION PROTEIN MUTANT E200K FRAGMENT 90-231 · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1FKC-1 RCSB PDB | nmr_structure | structure | in vitro · 25.85 °C · pH 4.6 HUMAN PRION PROTEIN (MUTANT E200K) FRAGMENT 90-231 · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1E1W-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein variant R220K · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1E1U-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein variant R220K · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1E1S-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein variant S170N · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1E1P-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein variant S170N · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1E1J-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein variant M166V · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-1E1G-1 RCSB PDB | nmr_structure | structure | in vitro · 19.85 °C · pH 4.5 Human prion protein variant M166V · PRION PROTEIN (chains A) | unmapped |
| EV-PDB-5L6R-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 4.9 PrP226* - Solution-state NMR structure of truncated human prion protein · Major prion protein (chains A) | unmapped |
| EV-PDB-5YJ4-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 4.5 structure for the protective mutant G127V of Human prion protein · Major prion protein (chains A) | unmapped |
| EV-PDB-5YJ5-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 4.5 structure for wildtype Human prion protein (M129) · Major prion protein (chains A) | unmapped |
| EV-PDB-6DU9-1 RCSB PDB | xray | resolution: 2.33 Å | in vitro · -173.15 °C · pH 7.6 · ligands CD, CL Crystal Structure of Human Prion Protein 90-231 · Major prion protein (chains A) | unmapped |
| EV-PDB-6LNI-1 RCSB PDB | cryoem | resolution: 2.702 Å | in vitro Cryo-EM structure of amyloid fibril formed by full-length human prion protein · Major prion protein (chains A,B,C,D,E,F,G,H,I,J) | unmapped |
| EV-PDB-6SUZ-1 RCSB PDB | xray | resolution: 2.5 Å | in vitro · 26.85 °C · ligands SO4 Human prion protein (PrP) fragment 119-231 (G127V V129 variant) complexed to ICSM 18 (anti-Prp therapeutic antibody) Fab fragment · Major prion protein (chains A) | unmapped |
| EV-PDB-6SV2-3 RCSB PDB | xray | resolution: 2.3 Å | in vitro · 26.85 °C · ligands SO4 Human prion protein (PrP) fragment 119-231 (G127V M129 variant) complexed to ICSM 18 (anti-Prp therapeutic antibody) Fab fragment · Major prion protein (chains A) | unmapped |
| EV-PDB-6UUR-1 RCSB PDB | cryoem | resolution: 3.5 Å | in vitro Human prion protein fibril, M129 variant · Major prion protein (chains A,B,C,D,E,F,G,H,I,J) | unmapped |
| EV-PDB-7DWV-1 RCSB PDB | cryoem | resolution: 3.07 Å | in vitro Cryo-EM structure of amyloid fibril formed by familial prion disease-related mutation E196K · Major prion protein (chains A,B,C,D,E,F) | unmapped |
| EV-PDB-7FHQ-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 4.5 Solution structure of the pathogenic mutant G131V of Human prion protein (91-231) · Major prion protein (chains A) | unmapped |
| EV-PDB-7RL4-1 RCSB PDB | cryoem | resolution: 2.86 Å | in vitro Cryo-EM structure of human PrP23-144 amyloid fibrils · Major prion protein (chains A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T) | unmapped |
| EV-PDB-7RVC-1 RCSB PDB | microed | resolution: 1.002 Å | in vitro · -173.15 °C · pH 4.5 Segment from the human prion protein 168-176 EYSNQNNFV · Major prion protein (chains A) | unmapped |
| EV-PDB-7RVE-1 RCSB PDB | microed | resolution: 0.85 Å | in vitro · -173.15 °C · pH 4.5 Segment from the S170N mutant of the human prion protein 168-176 EYNNQNNFV · Major prion protein (chains A) | unmapped |
| EV-PDB-7RVJ-1 RCSB PDB | microed | resolution: 1 Å | in vitro · -173.15 °C · pH 6.2 Segment from the human prion protein 169-175 YSNQNNF · Major prion protein (chains A,B) | unmapped |
| EV-PDB-7RVK-1 RCSB PDB | microed | resolution: 1 Å | in vitro · -173.15 °C · pH 6 · ligands ACT, ZN Segment from Y169G mutant of the human prion protein 169-175 GSNQNNF · Major prion protein (chains A) | unmapped |
| EV-PDB-7RVL-1 RCSB PDB | microed | resolution: 1 Å | in vitro · -173.15 °C · pH 4.5 Segment from the Y169F mutant of the human prion protein 168-176 EFSNQNNFV · Major prion protein (chains A) | unmapped |
| EV-PDB-7UMQ-1 RCSB PDB | cryoem | resolution: 3.29 Å | in vitro Structure of Type I Prion filaments from Gerstmann-Straussler-Scheinker disease · Major prion protein (chains A,B,C,D,E,F,G,H,I,J) | unmapped |
| EV-PDB-7UN5-1 RCSB PDB | cryoem | resolution: 3.13 Å | in vitro Structure of Type II Prion filaments from Gerstmann-Straussler-Scheinker disease · Major prion protein (chains A,B,C,D,E,F,G,H,I,J) | unmapped |
| EV-PDB-6PQA-1 RCSB PDB | xray | resolution: 1.46 Å | in vitro · -173.15 °C · pH 7 GAVVGG segment 119-124 from human prion · Major prion protein (chains A) | unmapped |
| EV-PDB-6PQ5-1 RCSB PDB | xray | resolution: 1.5 Å | in vitro · -173.15 °C · pH 4 · ligands MLI AGAAAA segment 113-118 from human prion · Major prion protein (chains A,B) | unmapped |
| EV-BMRB-15053 BMRB | nmr_shifts | chemical_shift | in vitro · 26.85 °C · pH 5 HPRP-173-195 SOLUTION STRUCTURE · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-15054 BMRB | nmr_shifts | chemical_shift | in vitro · 26.85 °C · pH 5 HPRP180-195 STRUCTURE · BMRB data: 1H chemical shifts | unmapped |
| EV-BMRB-16505 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 5 NMR structure of the octarepeat region of prion protein bound to pentosan polysulfate · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-16743 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 5.5 Three dimensional structure of HuPrP(90-231 M129 Q212P) · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17558 BMRB | nmr_shifts | chemical_shift | in vitro · 36.85 °C · pH 7.6 Structure of the CHR of the Prion protein in DPC Micelles · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17714 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 5.5 human prion protein mutant HuPrP(90-231, M129, V210I) · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17756 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 2 Backbone 1H and 13C Chemical Shift Assignments of human prion protein (residues 121-230) in its oxidized state · BMRB data: 13C chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17780 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 5.5 Human prion protein with E219K protective polymorphism · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-18426 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 5.5 Solution-state NMR structure of the human prion protein · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-18550 BMRB | nmr_shifts | chemical_shift | in vitro · -0.15 °C · pH 7.2 Solution-state NMR of prion protein mutant V210I at pH 7 · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-19268 BMRB | nmr_shifts | chemical_shift | in vitro · 25.85 °C · pH 4.6 SOLUTION NMR STRUCTURE OF THE V209M VARIANT OF THE HUMAN PRION PROTEIN (RESIDUES 90-231) · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-28115 BMRB | nmr_shifts | chemical_shift | in vitro · 5 °C · pH 4.5 Sequence-specific Backbone Resonance Assignments of Human PrP(23-144) at pH 4.5 · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-28116 BMRB | nmr_shifts | chemical_shift | in vitro · 5 °C · pH 7 Sequence-specific Backbone Resonance Assignments of Human PrP(23-144) at pH 7.0 · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-34003 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 4.9 PrP226* - Solution-state NMR structure of truncated human prion protein · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-36122 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 4.5 structure for the protective mutant G127V of Human prion protein · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-36123 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 4.5 structure for wildtype Human prion protein (M129) · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-4379 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C · pH 4.5 NMR Solution Structure of the Human Prion Protein Domain reveals Species Dependent Structural Disorder and Intramolecular Association with the Flexible Tail · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-4402 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C · pH 4.5 1H, 13C and 15N chemical shift assignment of human prion protein hPrP(23-230) · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-4434 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C · pH 4.5 NMR Solution Structure of the Human Prion Protein · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts | unmapped |
| EV-BMRB-4641 BMRB | nmr_shifts | chemical_shift | in vitro · 25.85 °C · pH 4.6 Human Prion Protein Mutant E200K Fragment 90-231 · BMRB data: 13C chemical shifts, 1H chemical shifts, 15N chemical shifts, coupling constants | unmapped |
| EV-BMRB-4736 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C · pH 4.5 1H, 13C, 15N Chemical Shift Assignment for the human prion protein variant M166V · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts | unmapped |
| EV-BMRB-50527 BMRB | nmr_shifts | chemical_shift | in vitro · 15.85 °C · pH 7 Backbone chemical shift assignments for the C-terminal domain of wild type human prion protein (residues 125-230) at 16deg C, pH 7. · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-50528 BMRB | nmr_shifts | chemical_shift | in vitro · 15.85 °C · pH 7 Backbone chemical shift assignments for the C-terminal domain of T183A human prion protein (residues 125-230) at 16deg C, pH 7. · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-5378 BMRB | nmr_shifts | chemical_shift | in vitro · 19.85 °C · pH 4.5 NMR Structure of a Variant Human Prion Protein with Two Disulfide Bridges · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts | unmapped |
| EV-BMRB-5713 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 7 Influence of pH on NMR structure and stability of the human prion protein globular domain · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-SASBDB-SASDMA7 SASBDB | saxs_sans | radius_of_gyration: 9.832 nm ± 0.036 | in vitro · 25 °C · pH 5 Structural characterization of beta-sheeted oligomers formed on the pathway of oxidative prion protein aggregation in vitro. · Major prion protein | unmapped |
| EV-SASBDB-SASDNB8 SASBDB | saxs_sans | radius_of_gyration: 2.83 nm ± 0.02 | in vitro · 20 °C · pH 7 A tetracationic porphyrin with dual anti-prion activity. · Major prion protein | unmapped |
| EV-SASBDB-SASDNC8 SASBDB | saxs_sans | radius_of_gyration: 3.1 nm ± 0.068 | in vitro · 20 °C · pH 7 A tetracationic porphyrin with dual anti-prion activity. · Major prion protein | unmapped |
| EV-SASBDB-SASDND8 SASBDB | saxs_sans | radius_of_gyration: 2.84 nm ± 0.022 | in vitro · 20 °C · pH 7 A tetracationic porphyrin with dual anti-prion activity. · Major prion protein | unmapped |
| EV-DISPROT-DP00466r003 DisProt | nmr_shifts | disorder_region: 102 residues | in vitro DisProt DP00466: disorder, residues 23-124 · residues 23-124; evidence: nuclear magnetic resonance spectroscopy evidence used in manual assertion | unmapped |
| EV-DISPROT-DP00466r006 DisProt | nmr_shifts | disorder_region: 102 residues | in vitro DisProt DP00466: disorder to order, residues 23-124 · residues 23-124; evidence: nuclear magnetic resonance evidence used in manual assertion | unmapped |
| EV-AFDB-AF-P04156-F1 AlphaFold DB | af_prediction | plddt: 64.19 pLDDT | in silico AlphaFold DB prediction AF-P04156-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-253 | unmapped |
| EV-SMASH-SMFS-000242 SMASH-BIO | force_spectroscopy | study_record | in vitro Quantifying the binding affinity of a pharmacological chaperone to transient unfolded states of a normally folded protein · Prion protein; optical tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-000464 SMASH-BIO | force_spectroscopy | study_record | in vitro How Sup35 monomer conformation and amyloid fibril polymorphism determine yeast strain phenotypes · Prion protein; optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-000732 SMASH-BIO | force_spectroscopy | study_record | in vitro Different folding mechanisms in prion proteins from mammals with different disease susceptibility observed at the single-molecule level · Prion protein; optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-001517 SMASH-BIO | force_spectroscopy | study_record | in vitro Following the Aggregation of Human Prion Protein on Heparin Functionalized Gold Surface in Real Time. · Prion protein; afm smfs; experiment class: membrane_mechanics, receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-002200 SMASH-BIO | force_spectroscopy | study_record | in vitro Unfolded and intermediate states of PrP play a key role in the mechanism of action of an antiprion chaperone. · Prion protein; optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003846 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Copper-induced structural conversion templates prion protein oligomerization and neurotoxicity. · Prion protein; afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003999 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7 Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein. · Prion protein; optical tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004340 SMASH-BIO | force_spectroscopy | study_record | in vitro Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape. · Prion protein; optical tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004359 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7 Role of monomer arrangement in the amyloid self-assembly. · Prion protein; afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004438 SMASH-BIO | force_spectroscopy | study_record | in vitro β-sheet-like formation during the mechanical unfolding of prion protein. · Prion protein; force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004879 SMASH-BIO | force_spectroscopy | study_record | in vitro Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition. · Prion protein; afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005158 SMASH-BIO | force_spectroscopy | study_record | in vitro Direct observation of multiple misfolding pathways in a single prion protein molecule. · Prion protein; optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005171 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7 Effect of electrostatics on aggregation of prion protein Sup35 peptide. · Prion protein; afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005184 SMASH-BIO | force_spectroscopy | study_record | in vitro Energy landscape analysis of native folding of the prion protein yields the diffusion constant, transition path time, and rates. · Prion protein; optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005602-r0 SMASH-BIO | force_spectroscopy | persistence_length: 1.5 µm | in vitro Physical properties of polymorphic yeast prion amyloid fibers. · Prion protein; optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005877 SMASH-BIO | force_spectroscopy | study_record | in vitro Optical trapping with high forces reveals unexpected behaviors of prion fibrils. · Prion protein; optical tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-006398 SMASH-BIO | force_spectroscopy | study_record | in vitro Nanomechanical properties of human prion protein amyloid as probed by force spectroscopy. · Prion protein; afm smfs; experiment class: unfolding_protein | unmapped |
Conflicts
No conflicts found among comparable evidence.
117 evidence items could not be compared: they lack a comparable observable type, a value, or an uncertainty. Absence of a conflict here is not agreement.