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DPC micelle-bound NMR structures of Tritrp3
Authors
Schibli, D.J., Nguyen, L.T.
Assembly
13-mer analogue of Prophenin-1 containing WWW
Entity
1. 13-mer analogue of Prophenin-1 containing WWW (polymer, Thiol state: not present), 14 monomers, 1848.187 Da Detail

VRRFAWWWAF LRRX


Formula weight
1848.187 Da
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 92.9 %, Completeness: 85.3 %, Completeness (bb): 92.3 % Detail

Polymer type: polypeptide(L)

Total1H
All85.3 % (87 of 102)85.3 % (87 of 102)
Backbone92.3 % (24 of 26)92.3 % (24 of 26)
Sidechain82.9 % (63 of 76)82.9 % (63 of 76)
Aromatic89.3 % (25 of 28)89.3 % (25 of 28)
Methyl66.7 % (4 of 6)66.7 % (4 of 6)

1. 13-mer analogue of Prophenin-1 containing WWW

VRRFAWWWAF LRRX

Sample

Solvent system 90% H2O, 10% D2O, Temperature 310 K, pH 4.7, Details 90% H2O, 10% D2O, 132 mM DPC-d38


#NameIsotope labelingTypeConcentration
1Tritrp3natural abundance1.0 ~ 2.0 mM
2DPC-d38132 mM
3H2O90 %
4D2O10 %

Protein Blocks Logo
Calculated from 20 models in PDB: 2I1F, Strand ID: A Detail


Release date
2007-10-29
Citation
Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures
Schibli, D.J., Nguyen, L.T., Kernaghan, S.D., Rekdal, O., Vogel, H.J.
Biophys. J. (2006), 91, 4413-4426, PubMed 16997878 , DOI 10.1529/biophysj.106.085837 ,
Related entities 1. 13-mer analogue of Prophenin-1 containing WWW, : 1 : 2 : 4 entities Detail
Experiments performed 3 experiments Detail
nullKeywords antimicrobial peptide, micelle-bound peptide, turn