2mn8

NMR structure of a peptoid analogue of maculatin G15 containing cis-Nleu at position 13

spinqualitylabelsall models 2mn8 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mn8 is a 1 chain structure with sequence from Ranoidea genimaculata. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Ligands: I4G, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MCU11_RANGE Publication Abstract from PubMed 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. Structural features of peptoid-peptide hybrids in lipid-water interfaces.,Uggerhoj LE, Munk JK, Hansen PR, Guntert P, Wimmer R FEBS Lett. 2014 Aug 25;588(17):3291-7. doi: 10.1016/j.febslet.2014.07.016. Epub, 2014 Jul 22. PMID:25063337 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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