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==SOLUTION NMR STRUCTURE OF MAXIMIN 1 IN 50% TRIFLUOROETHANOL==
<StructureSection load='7ovz' size='340' side='right'caption='[[7ovz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OVZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ovz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ovz OCA], [https://pdbe.org/7ovz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ovz RCSB], [https://www.ebi.ac.uk/pdbsum/7ovz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ovz ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Maximin 1 is a cationic, amphipathic antimicrobial peptide found in the skin secretions and brains of the Chinese red belly toad Bombina maxima. The 27 amino acid residue-long peptide is biologically interesting as it possesses a variety of biological activities, including antibacterial, antifungal, antiviral, antitumour and spermicidal activities. Its three-dimensional structural model was obtained in a 50/50% water/2,2,2-trifluoroethanol-d3 mixture using two-dimensional NMR spectroscopy. Maximin 1 was found to adopt an alpha-helical structure from residue Ile(2) to Ala(26) . The peptide is amphipathic, showing a clear separation between polar and non-polar residues. The interactions with sodium dodecyl sulfate micelles, a widely-used bacterial membrane-mimicking environment, were modelled using molecular dynamics simulations. The peptide maintains an alpha-helical conformation, occasionally displaying a flexibility around the Gly(9) and Gly(16) residues, which is likely responsible for the peptide's low haemolytic activity. It is found to preferentially adopt a position parallel to the micellar surface, establishing a number of hydrophobic and electrostatic interactions with the micelle.

Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1.,Timmons PB, Hewage CM J Pept Sci. 2021 Sep 26:e3370. doi: 10.1002/psc.3370. PMID:34569121<ref>PMID:34569121</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Hewage CM]]
[[Category: Timmons PB]]