1dhl: Difference between revisions

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 {{Theoretical_model}}
-{{Seed}}
-[[Image:1dhl.png|left|200px]]
-<!--
+==MODELS OF DELTA-HEMOLYSIN MEMBRANE CHANNELS AND CRYSTAL STRUCTURES==
-The line below this paragraph, containing "STRUCTURE_1dhl", creates the "Structure Box" on the page.
+<StructureSection load='1dhl' size='340' side='right'caption='[[1dhl]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DHL FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=1dhl FirstGlance], [https://www.ebi.ac.uk/pdbsum/1dhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dhl ProSAT]</span></td></tr>
--->
+</table>
-{{STRUCTURE_1dhl|  PDB=1dhl  |  SCENE=  }}
+<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.
-===MODELS OF DELTA-HEMOLYSIN MEMBRANE CHANNELS AND CRYSTAL STRUCTURES===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_2281085}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1dhl" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 2281085 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_2281085}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHL OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:2281085</ref><references group="xtra"/>
 [[Category: Guy, H R]]
 [[Category: Raghunathan, G]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 07:09:39 2010''