| 2mag >> Magainin 2 |
|---|
| Hydrophobic Thickness or Depth | 10.1 Å |
| Tilt Angle | 81° |
| ΔGtransfer | -13.7 kcal/mol |
| Links to 2mag | PDB Sum, PDB, MSD, MMDB |
| Topology | outer side |
| Resolution | NMR |
| Primary PDB represention | 2mag |
| Other PDB entries representing this structure | 1dum (NMR), 2lsa (NMR) |
| Number of TM secondary structures | 0 |
| Membranome | |
| Uniprot | MAGA_XENLA |
  | outer side |
| inner side |
Comments: Antimicrobial peptide that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. This peptide forms oligomeric ion channels in membranes. It also forms a dimer (1dum). Structure in SDS micelles (2lsa too).
| Verification: Magainin 2 |
|---|
| The alpha-helix of magainin is parallel to the membrane surface, with its nonpolar side (F5, L6, F16, I20) buried in the hydrophobic region of the membrane (Matsuzaki et al. 1994, Marassi et al. 2000). The transfer energy is strongly overestimated (~ -8 kcal/mol in the experiment, Wieprecht et al. 1999), because part of the transfer energy must be spent to fold an alpha-helix from a coil in aqueous solution, prior to insertion of the helix into membrane. |
| References: 3 |
|---|
| Matsuzaki K, Murase O, Tokuda H, Funakoshi S, Fujii N, and Miyajima K. 1994 Orientational and aggregational states of magainin 2 in phospholipid bilayers. Biochemistry. 33: 3342-3349. PubMed |
| Marassi FM, Ma C, Gesell JJ, and Opella SJ. 2000. Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonances from in-plane residues in uniformly (15)N-labeled helical membrane proteins in oriented lipid bilayers. J Magn Reson PubMed |
| Wieprecht, T., Beyermann, M., and Seelig, J. 1999. Binding of antibacterial magainin peptides to electrically neutral membranes: thermodynamics and structure. Biochemistry. 38:10377-10387. PubMed |
