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HPRP180-195 STRUCTURE
Authors
Saviano, G., Tancredi, T.
Assembly
HPRP-180-195 PEPTIDE
Entity
1. HPRP-180-195 PEPTIDE (polymer, Thiol state: all free), 16 monomers, 1741.980 Da Detail

VNITIKQHTV TTTTKG


Formula weight
1741.98 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 83.5 %, Completeness (bb): 93.9 % Detail

Polymer type: polypeptide(L)

Total1H
All83.5 % (76 of 91)83.5 % (76 of 91)
Backbone93.9 % (31 of 33)93.9 % (31 of 33)
Sidechain77.6 % (45 of 58)77.6 % (45 of 58)
Aromatic100.0 % (2 of 2)100.0 % (2 of 2)
Methyl92.9 % (13 of 14)92.9 % (13 of 14)

1. HPRP-180-195 PEPTIDE

VNITIKQHTV TTTTKG

Sample

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


#NameIsotope labelingTypeConcentration
1HPRP-180-195 PEPTIDEnatural 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: 15053 released on 2007-01-31
    Title HPRP-173-195 SOLUTION STRUCTURE
Related entities 1. HPRP-180-195 PEPTIDE, : 1 : 92 : 50 : 1 : 2 entities Detail
Interaction partners 1. HPRP-180-195 PEPTIDE, : 68 interactors Detail
Experiments performed 4 experiments Detail
Chemical shift validation 3 contents Detail
Keywords ALPHA2-HELIX, HUMAN PRION PROTEIN