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The peptide Lt-MAP4 is an analog derived from the Ltc-3a. The primary sequence of the parental peptide was used as template for rational design, using the amino acid residues for modification of charge and hydrophobicity.
Authors
Freitas, C.D.P., Moraes, L.F.R.N., Migliolo, L., Liao, L.M.
Assembly
Lt-MAP4 (LKKLWRFLKKL)
Entity
1. Lt-MAP4 (LKKLWRFLKKL) (polymer, Thiol state: not present), 11 monomers, 1472.902 Da Detail

LKKLWRFLKK L


Formula weight
1472.902 Da
Source organism
Lachesana tarabaevi
Exptl. method
solution NMR
Data set
assigned_chemical_shifts, spectral_peak_list
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 72.1 %, Completeness (bb): 72.7 % Detail

Polymer type: polypeptide(L)

Total1H13C
All72.1 % (119 of 165)84.4 % (81 of 96)55.1 % (38 of 69)
Backbone72.7 % (40 of 55)95.5 % (21 of 22)57.6 % (19 of 33)
Sidechain71.9 % (87 of 121)81.1 % (60 of 74)57.4 % (27 of 47)
Aromatic52.4 % (11 of 21)54.5 % (6 of 11)50.0 % (5 of 10)
Methyl75.0 % (12 of 16)75.0 % (6 of 8)75.0 % (6 of 8)

1. entity 1

LKKLWRFLKK L

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 313 K, pH 4.46, Details 1 mM Latarasin-L4, 100 mM [U-98% 2H] SDS-d25, 0.035 % [U-98% 2H] DSS-d6, 90% H2O/10% D2O


#NameIsotope labelingTypeConcentration
1Latarasin-L4natural abundance1 mM
2SDS-d25[U-98% 2H]100 mM
3DSS-d6[U-98% 2H]0.035 %

Release date
2022-01-13
Citation
Two-dimensional NMR structural study of latarasin analogue Lt-MAP4 multifunctional synthetic peptide
Freitas, C.D.P., Liao, L.M., Migliolo, L., Moraes, L.F.R.N.
Experiments performed 3 experiments Detail
nullKeywords AMPs, STRUCTURAL PROTEIN