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1pef

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[[Image:1pef.jpg|left|200px]]
 
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==PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE==
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The line below this paragraph, containing "STRUCTURE_1pef", creates the "Structure Box" on the page.
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<StructureSection load='1pef' size='340' side='right'caption='[[1pef]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<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>
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{{STRUCTURE_1pef| PDB=1pef | SCENE= }}
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</table>
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__TOC__
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'''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE'''
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Garavito RM]]
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==Overview==
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[[Category: Taylor K]]
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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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[[Category: Yang NC]]
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==About this Structure==
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEF OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8868477 8868477]
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[[Category: Garavito, R M.]]
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[[Category: Taylor, K.]]
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[[Category: Yang, N C.]]
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[[Category: Alpha-helical bundle]]
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[[Category: Synthetic protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:59:38 2008''
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Current revision

PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE

PDB ID 1pef

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