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| [[Image:1pef.jpg|left|200px]]
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| {{Structure
| | ==PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE== |
| |PDB= 1pef |SIZE=350|CAPTION= <scene name='initialview01'>1pef</scene>, resolution 1.5Å
| | <StructureSection load='1pef' size='340' side='right'caption='[[1pef]], [[Resolution|resolution]] 1.50Å' scene=''> |
| |SITE=
| | == Structural highlights == |
| |LIGAND=
| | <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> |
| |ACTIVITY=
| | </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> |
| |GENE=
| | <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> |
| |DOMAIN=
| | </table> |
| |RELATEDENTRY=
| | __TOC__ |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pef OCA], [http://www.ebi.ac.uk/pdbsum/1pef PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pef RCSB]</span>
| | </StructureSection> |
| }}
| | [[Category: Large Structures]] |
| | | [[Category: Garavito RM]] |
| '''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE'''
| | [[Category: Taylor K]] |
| | | [[Category: Yang NC]] |
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| ==Overview==
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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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| ==About this Structure==
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| 1PEF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. 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: Protein complex]] | |
| [[Category: Garavito, R M.]] | |
| [[Category: Taylor, K.]] | |
| [[Category: Yang, N C.]] | |
| [[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 Sun Mar 30 22:58:40 2008''
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