5mxt: Difference between revisions

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<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=5mxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mxt OCA], [http://pdbe.org/5mxt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mxt RCSB], [http://www.ebi.ac.uk/pdbsum/5mxt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mxt ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Certain cationic peptides interact with biological membranes. These often-complex interactions can result in peptide targeting to the membrane, or in membrane permeation, rupture, and cell lysis. We investigated the relationship between the structural features of membrane-active peptides and these effects, to better understand these processes. To this end, we employed a computational method for morphing a membranolytic antimicrobial peptide into a nonmembranolytic mitochondrial targeting peptide by "directed simulated evolution." The results obtained demonstrate that superficially subtle sequence modifications can strongly affect the peptides' membranolytic and membrane-targeting abilities. Spectroscopic and computational analyses suggest that N- and C-terminal structural flexibility plays a crucial role in determining the mode of peptide-membrane interaction.

Peptide-Membrane Interaction between Targeting and Lysis.,Stutz K, Muller AT, Hiss JA, Schneider P, Blatter M, Pfeiffer B, Posselt G, Kanfer G, Kornmann B, Wrede P, Altmann KH, Wessler S, Schneider G ACS Chem Biol. 2017 Aug 8. doi: 10.1021/acschembio.7b00504. PMID:28763193<ref>PMID:28763193</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 7: / Line 7: @@
 <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=5mxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mxt OCA], [http://pdbe.org/5mxt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mxt RCSB], [http://www.ebi.ac.uk/pdbsum/5mxt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mxt ProSAT]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Certain cationic peptides interact with biological membranes. These often-complex interactions can result in peptide targeting to the membrane, or in membrane permeation, rupture, and cell lysis. We investigated the relationship between the structural features of membrane-active peptides and these effects, to better understand these processes. To this end, we employed a computational method for morphing a membranolytic antimicrobial peptide into a nonmembranolytic mitochondrial targeting peptide by "directed simulated evolution." The results obtained demonstrate that superficially subtle sequence modifications can strongly affect the peptides' membranolytic and membrane-targeting abilities. Spectroscopic and computational analyses suggest that N- and C-terminal structural flexibility plays a crucial role in determining the mode of peptide-membrane interaction.
+Peptide-Membrane Interaction between Targeting and Lysis.,Stutz K, Muller AT, Hiss JA, Schneider P, Blatter M, Pfeiffer B, Posselt G, Kanfer G, Kornmann B, Wrede P, Altmann KH, Wessler S, Schneider G ACS Chem Biol. 2017 Aug 8. doi: 10.1021/acschembio.7b00504. PMID:28763193<ref>PMID:28763193</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5mxt" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>