1pef: Difference between revisions

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[[Image:1pef.jpg|left|200px]]


{{Structure
==PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE==
|PDB= 1pef |SIZE=350|CAPTION= <scene name='initialview01'>1pef</scene>, resolution 1.5&Aring;
<StructureSection load='1pef' size='340' side='right'caption='[[1pef]], [[Resolution|resolution]] 1.50&Aring;' 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]] 1.5&#8491;</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>
}}
</table>
 
__TOC__
'''PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE'''
</StructureSection>
 
[[Category: Large Structures]]
 
[[Category: Garavito RM]]
==Overview==
[[Category: Taylor K]]
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.
[[Category: Yang NC]]
 
==About this Structure==
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].  
 
==Reference==
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]
[[Category: Protein complex]]
[[Category: Garavito, R M.]]
[[Category: Taylor, K.]]
[[Category: Yang, N C.]]
[[Category: alpha-helical bundle]]
[[Category: synthetic protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:23:19 2008''

Latest revision as of 08:07, 14 February 2024

PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE

1pef, resolution 1.50Å

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