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The design of the beta-harpin and a-helix tethered by a 4Gly linker using conformationally restricted libraries
Authors
Pantoja-Uceda, D., Pineda-Lucena, A.
Assembly
MHB4A
Entity
1. MHB4A (polymer, Thiol state: not present), 33 monomers, 3435.779 Da Detail

RGKWTYNGIT YEGGGGSAAE AYAKRIAEAM AKG


Formula weight
3435.779 Da
Exptl. method
NMR
Refine. method
torsion angle dynamics
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 87.9 %, Completeness: 87.8 %, Completeness (bb): 84.9 % Detail

Polymer type: polypeptide(L)

Total1H
All87.8 % (159 of 181)87.8 % (159 of 181)
Backbone84.9 % (62 of 73)84.9 % (62 of 73)
Sidechain89.8 % (97 of 108)89.8 % (97 of 108)
Aromatic100.0 % (18 of 18)100.0 % (18 of 18)
Methyl100.0 % (13 of 13)100.0 % (13 of 13)

1. MHB4A

RGKWTYNGIT YEGGGGSAAE AYAKRIAEAM AKG

Sample

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


#NameIsotope labelingTypeConcentration
1MHB4Aprotein1.5 mM

Protein Blocks Logo
Calculated from 20 models in PDB: 2I9N, 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 ,
Related entities 1. MHB4A, : 1 : 1 entities Detail
Experiments performed 2 experiments Detail
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