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HPRP-173-195 SOLUTION STRUCTURE
Authors
Saviano, G., Tancredi, T.
Assembly
prion protein fragment
Entity
1. prion protein fragment (polymer, Thiol state: all free), 23 monomers, 2571.859 Da Detail

NNFVHDCVNI TIKQHTVTTT TKG


Formula weight
2571.859 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 84.0 %, Completeness (bb): 100.0 % Detail

Polymer type: polypeptide(L)

Total1H
All84.0 % (110 of 131)84.0 % (110 of 131)
Backbone100.0 % (47 of 47)100.0 % (47 of 47)
Sidechain75.0 % (63 of 84)75.0 % (63 of 84)
Aromatic44.4 % (4 of 9)44.4 % (4 of 9)
Methyl75.0 % (12 of 16)75.0 % (12 of 16)

1. HPRP173195

NNFVHDCVNI TIKQHTVTTT TKG

Sample

Pressure 1.0 atm, Temperature 300.0 K, pH 5.0, Details TRIFLUOROETHANOL-D2


#NameIsotope labelingTypeConcentration
1HPRP173195natural abundance1.0 ~ 2.0 mM
2TRIFLUOROETHANOL-D2[U-2H]100 %

Release date
2007-01-31
Citation
Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein alpha 2-helical 180-195 segment, and comparison with full-length alpha 2-helix-derived peptides
Ronga, L., Palladino, P., Saviano, G., Tancredi, T., Benedetti, E., Ragone, R., Rossi, F.
J. Pept. Sci. (2008), 14, 1096-1102, PubMed 18563793 , DOI 10.1002/psc.1046 ,
Entries sharing articles BMRB: 2 entries Detail
  BMRB: 15052 released on 2007-01-31
    Title HPRP-173-195-D178N SOLUTION STRUCTURE
  BMRB: 15054 released on 2007-01-31
    Title HPRP180-195 STRUCTURE
Related entities 1. prion protein fragment, : 1 : 83 : 44 : 5 : 15 entities Detail
Interaction partners 1. prion protein fragment, : 68 interactors Detail
Experiments performed 4 experiments Detail
Chemical shift validation 3 contents Detail
Keywords HUMAN PRION PROTEIN, NMR, PEPTIDE, SOLUTION STRUCTURE