STRUCTURE OF THE BOVINE ANTIMICROBIAL PEPTIDE INDOLICIDIN BOUND TO DODECYLPHOSPHOCHOLINE MICELLES
Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles.
Same peptide complexed with sodium dodecyl sulfate micelles.
The peptide was chemically synthesized. The sequence occurs naturally in Bos taurus (bovine) neutrophils. The sequence is naturally amidated at the C-terminus.
This structure was determined using standard 2D homonuclear techniques.
structures with the least restraint violations,structures with the lowest energy
The structures are based on 118 (non-redundant) NOE-derived distance restraints, 61 inter-residue and 57 intra-residue
distance geometry and simulated annealing
2 mM indolicidin; 400 mM dodecylphosphocholine
poly-L-proline II helix, half turn, ANTIMICROBIAL PROTEIN