Description
Experimental Technique/Method:SOLUTION NMR
Resolution:
Classification:ANTIMICROBIAL PROTEIN
Release Date:2014-07-23
Deposition Date:2014-03-29
Revision Date:2014-12-03
Molecular Weight:2121.53
Macromolecule Type:Protein
Residue Count:22
Atom Site Count:151
DOI:10.2210/pdb2mn9/pdb
Abstract:
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 α-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.
Resolution:
Classification:ANTIMICROBIAL PROTEIN
Release Date:2014-07-23
Deposition Date:2014-03-29
Revision Date:2014-12-03
Molecular Weight:2121.53
Macromolecule Type:Protein
Residue Count:22
Atom Site Count:151
DOI:10.2210/pdb2mn9/pdb
Abstract:
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 α-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.
| Date made available | 23 Jul 2014 |
|---|---|
| Publisher | RCSB-PDB |