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DPC micelle-bound NMR structures of Tritrp1
Authors
Schibli, D.J., Nguyen, L.T.
Assembly
Prophenin1
Entity
1. Prophenin1 (polymer, Thiol state: not present), 14 monomers, 1900.261 Da Detail

VRRFPWWWPF LRRX


Formula weight
1900.261 Da
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 92.9 %, Completeness: 84.5 %, Completeness (bb): 95.8 % Detail

Polymer type: polypeptide(L)

Total1H
All84.5 % (93 of 110)84.5 % (93 of 110)
Backbone95.8 % (23 of 24)95.8 % (23 of 24)
Sidechain81.4 % (70 of 86)81.4 % (70 of 86)
Aromatic85.7 % (24 of 28)85.7 % (24 of 28)
Methyl50.0 % (2 of 4)50.0 % (2 of 4)

1. Prophenin1

VRRFPWWWPF LRRX

Sample

Solvent system 90% H2O, 10% D2O, Temperature 310 K, pH 4.5, Details 90% H2O, 10% D2O, 150 mM DPC-d38


#NameIsotope labelingTypeConcentration
1Tritrp1natural abundance1.0 ~ 3.0 mM
2DPC-d38150 mM
3H2O90 %
4D2O10 %

Protein Blocks Logo
Calculated from 20 models in PDB: 2I1D, Strand ID: A Detail


Release date
2007-01-09
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. Prophenin1, : 1 : 5 : 3 entities Detail
Experiments performed 3 experiments Detail
nullKeywords antimicrobial peptide, micelle-bound peptide, turn