3dhl
From Proteopedia
(Difference between revisions)
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</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=3dhl FirstGlance], [https://www.ebi.ac.uk/pdbsum/3dhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dhl ProSAT]</span></td></tr> | </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=3dhl FirstGlance], [https://www.ebi.ac.uk/pdbsum/3dhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dhl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Molecular modeling and energy calculations have been used to study how delta-hemolysin and melittin helices may aggregate on membrane surfaces and insert through membranes to form channels. In these models adjacent antiparallel amphipathic helices form planar "raft" structures, in which one surface is hydrophobic and the other hydrophilic. Models of delta-hemolysin crystal structure were developed using these "rafts." These models are based on the unit cell constants and the crystal symmetry obtained from the preliminary crystal data. Energy calculations favor channel models of delta-hemolysin with six or eight monomers per channel. | ||
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| - | Models of delta-hemolysin membrane channels and crystal structures.,Raghunathan G, Seetharamulu P, Brooks BR, Guy HR Proteins. 1990;8(3):213-25. PMID:2281085<ref>PMID:2281085</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3dhl" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
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MODELS OF DELTA-HEMOLYSIN MEMBRANE CHANNELS AND CRYSTAL STRUCTURES
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