Magainin 2: Difference between revisions

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==Introduction==
==Introduction==
Magainin are a class of antimicrobial peptides (AMPs) found in the African clawed frog Xenopus Laevis.  
'''Magainin''' are a class of antimicrobial peptides (AMPs) found in the African clawed frog Xenopus Laevis.  
AMPs consists of 10-50 amino acids, and are produced by Eukaryotes, as part of their defence mechanism from bacteria. For informatoin about AMPs you can visit the Proteopedia page [[Antimicrobial peptides]]
AMPs consists of 10-50 amino acids, and are produced by Eukaryotes, as part of their defence mechanism from bacteria. For informatoin about AMPs you can visit the Proteopedia page [[Antimicrobial peptides]]
 Magainin 1 and 2 were discovered by Dr. Michael Zasloff and first reported in 1987. They have an alpha helix structure, and are water soluble and Potentially amphiphilic.
 Magainin 1 and 2 were discovered by Dr. Michael Zasloff and first reported in 1987. They have an alpha helix structure, and are water soluble and Potentially amphiphilic.
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</StructureSection>
</StructureSection>
==3D structures of magainin 2==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[2mag]], [[2lsa]] – Mag2 – frog - NMR<br />
[[1dum]] – Mag2 (mutant) - NMR<br />
[[4mgp]], [[5cgn]], [[5cgo]] – Mag2 (mutant) <br />
[[1d9j]], [[1d9l]], [[1d9o]], [[1d9m]], [[1d9p]], [[1f0d]], [[1f0e]], [[1f0f]], [[1f0g]], [[1f0h]] – Mag2/cecropin A - NMR<br />
== References ==
== References ==
1-'''J. Gesella., M. Zasloffb and S. J. Opellaa'''., Two-dimensional H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. ''Journal of Biomolecular NMR'', 1997. 9: 127–135.
1-'''J. Gesella., M. Zasloffb and S. J. Opellaa'''., Two-dimensional H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. ''Journal of Biomolecular NMR'', 1997. 9: 127–135.