1dum

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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dum OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dum RCSB], [http://www.ebi.ac.uk/pdbsum/1dum PDBsum]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dum OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dum RCSB], [http://www.ebi.ac.uk/pdbsum/1dum PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/MAGA_XENLA MAGA_XENLA]] Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Magainins are membrane lytic agents.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 12:48, 25 December 2014

NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES

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