Search

Design of a-helical peptide based on conformationally restricted libraries
Authors
Pantoja-Uceda, D., Pineda-Lucena, A.
Assembly
MHA6
Entity
1. MHA6 (polymer, Thiol state: not present), 17 monomers, 1737.973 Da Detail

SAAEAYAKRI AEAMAKG


Formula weight
1737.973 Da
Exptl. method
NMR
Refine. method
torsion angle dynamics
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 78.1 %, Completeness (bb): 74.1 % Detail

Polymer type: polypeptide(L)

Total1H13C
All78.1 % (125 of 160)97.8 % (89 of 91)52.2 % (36 of 69)
Backbone74.1 % (63 of 85)100.0 % (35 of 35)56.0 % (28 of 50)
Sidechain78.0 % (71 of 91)96.4 % (54 of 56)48.6 % (17 of 35)
Aromatic50.0 % (4 of 8)100.0 % (4 of 4) 0.0 % (0 of 4)
Methyl55.6 % (10 of 18)100.0 % (9 of 9)11.1 % (1 of 9)

1. MH6A

SAAEAYAKRI AEAMAKG

Sample

Temperature 283.0 (±0.1) K, pH 5.0 (±0.1)


#NameIsotope labelingTypeConcentration
1MH6Aprotein1.5 mM

Protein Blocks Logo
Calculated from 20 models in PDB: 2I9M, Strand ID: A Detail


Release date
2008-05-21
Citation
Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously
Pantoja-Uceda, D., Pastor, Salgado, J., Pineda-Lucena, A., Perez-Paya, E.
J. Pept. Sci. (2008), 14, 845-854, PubMed 18247449 , DOI 10.1002/psc.1015 ,
Entries sharing articles BMRB: 2 entries Detail
  BMRB: 7283 released on 2008-05-21
    Title The design of the beta-harpin and a-helix tethered by a 4Gly linker using conformationally restricted libraries
  BMRB: 7284 released on 2008-05-21
    Title The design of the beta-harpin and a-helix tethered by a 4Gly linker using conformationally restricted libraries
Related entities 1. MHA6, : 1 : 2 entities Detail
Experiments performed 3 experiments Detail
null