2MMJ: Structure of a peptoid analogue of maculatin G15 in DPC micelles

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: 2MMJDownload
MMDB ID: 121631
PDB Deposition Date: 2014/3/15
Updated in MMDB: 2014/12
Experimental Method:
solution nmr
Similar Structures:
Biological Unit for 2MMJ: monomeric; determined by author
Molecular Components in 2MMJ
Label Count Molecule
Protein (1 molecule)
Maculatin G15
Molecule annotation
Chemical (1 molecule)
Molecule information is not avaliable.
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Citing MMDB