2MN9: peptoid analogue of maculatin G15 - peptoid trans-Nleu at position 13

The inclusion of peptoid monomers into antimicrobial peptides (AMPs) increases their proteolytic resistance, but introduces conformational flexibility (reduced hydrogen bonding ability and cis/trans isomerism). We here use NMR spectroscopy to answer how the insertion of a peptoid monomer influences the structure of a regular alpha-helical AMP upon interaction with a dodecyl phosphocholine (DPC) micelle. Insertion of [(2-methylpropyl)amino]acetic acid in maculatin-G15 shows that the structural change and conformational flexibility depends on the site of insertion. This is governed by the micelle interaction of the amphipathic helices flanking the peptoid monomer and the side chain properties of the peptoid and its preceding residue.
PDB ID: 2MN9Download
MMDB ID: 121633
PDB Deposition Date: 2014/3/29
Updated in MMDB: 2014/12
Experimental Method:
solution nmr
Similar Structures:
Biological Unit for 2MN9: monomeric; determined by author
Molecular Components in 2MN9
Label Count Molecule
Protein (1 molecule)
Maculatin G15
Molecule annotation
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Citing MMDB