This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1pef
From Proteopedia
(Difference between revisions)
m (Protected "1pef" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | [[ | + | ==PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE== |
| + | <StructureSection load='1pef' size='340' side='right' caption='[[1pef]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PEF FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1pef RCSB], [http://www.ebi.ac.uk/pdbsum/1pef PDBsum]</span></td></tr> | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Garavito, R M.]] | [[Category: Garavito, R M.]] | ||
[[Category: Taylor, K.]] | [[Category: Taylor, K.]] | ||
Revision as of 06:48, 9 June 2014
PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE
| |||||||||||
