NMR structure of antimicrobial peptide distinctin in water
A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin.
A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta
HELIX DETERMINATION METHOD: AUTHOR DETERMINED
The peptide was prepared by solid-phase synthesis. This sequence occurs naturally in the tree-frog Phyllomedusa distincta
This structure was determined using standard 2D homonuclear techniques.
Structures within a prefixed threshold of amber energy, solvent accessible surface area and symmetry-based penalty functions (see jrnl)
the structures are based on a total of 636 restraints, 548 are NOE-derived distance constraints, 88 distance restraints from hydrogen bonds.
simulated annealing with cartesian coordinate dynamics
structure within a prefixed threshold of amber energy, solvent accessible surface area and symmetry-based penalty functions
3.8mM Natural Abundance Distinctin; NaN3
0.05mM Natural Abundance Distinctin; NaN3
PORE-FORMING PEPTIDE, HETERODIMER, HOMODIMER, DISULFIDE, FOUR-HELIX BUNDLE, ANTIBIOTIC