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1pef
From Proteopedia
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==PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE== | ==PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE== | ||
| - | <StructureSection load='1pef' size='340' side='right' caption='[[1pef]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='1pef' size='340' side='right'caption='[[1pef]], [[Resolution|resolution]] 1.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1pef]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEF OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[1pef]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PEF FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</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=1pef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pef OCA], [https://pdbe.org/1pef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pef RCSB], [https://www.ebi.ac.uk/pdbsum/1pef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pef ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | X-ray diffraction analysis at 1.5 A resolution has confirmed the helical conformation of a de novo designed 18-residue peptide. However, the crystal structure reveals the formation of continuous molecular layers of parallel-packed amphiphilic helices as a result of much more extensive helix-helix interactions than predicted. The crystal packing arrangement, by virtue of distinct antiparallel packing interactions, segregates the polar and apolar surfaces of the helices into discrete and well-defined interfacial regions. An extensive "ridges-into-grooves" interdigitation characterizes the hydrophobic interface, whereas an extensive network of salt bridges and hydrogen bonds dominates the corresponding hydrophilic interface. | ||
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| - | A novel, multilayer structure of a helical peptide.,Taylor KS, Lou MZ, Chin TM, Yang NC, Garavito RM Protein Sci. 1996 Mar;5(3):414-21. PMID:8868477<ref>PMID:8868477</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1pef" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Garavito RM]] |
| - | [[Category: | + | [[Category: Taylor K]] |
| - | [[Category: | + | [[Category: Yang NC]] |
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Current revision
PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE
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