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Conformational and membrane interactins studies of antimicrobial peptide Alyteserin-1C
Authors
Subasinghage, A.P., Hewage, C.M., Conlon, M.
Assembly
Alyteserin-1C
Entity
1. Alyteserin-1C (polymer, Thiol state: not present), 23 monomers, 2266.680 Da Detail

GLKEIFKAGL GSLVKGIAAH VAS


Formula weight
2266.68 Da
Source organism
Alytes obstetricans
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 82.0 %, Completeness (bb): 98.0 % Detail

Polymer type: polypeptide(L)

Total1H
All82.0 % (105 of 128)82.0 % (105 of 128)
Backbone98.0 % (49 of 50)98.0 % (49 of 50)
Sidechain71.8 % (56 of 78)71.8 % (56 of 78)
Aromatic28.6 % (2 of 7)28.6 % (2 of 7)
Methyl94.4 % (17 of 18)94.4 % (17 of 18)

1. Alyteserin-1C

GLKEIFKAGL GSLVKGIAAH VAS

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 307 K, pH 3.5, Details DHPC was used as micelles


#NameIsotope labelingTypeConcentration
1DHPCnatural abundance290 mM
2H2Onatural abundance90 %
3D2Onatural abundance10 %
4Alyteserin-1Cnatural abundance1.54 mM

Protein Blocks Logo
Calculated from 20 models in PDB: 2L5R, Strand ID: A Detail


Release date
2011-05-17
Citation
Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K]alyteserin-1c
Subasinghage, A.P., Conlon, D., Hewage, J.
Biochim. Biophys. Acta (2011), 1808, 1975-1984, PubMed 21565166 , DOI 10.1016/j.bbamem.2011.04.012 ,
Related entities 1. Alyteserin-1C, : 1 entities Detail
Experiments performed 2 experiments Detail
nullKeywords alpha helix