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.
1j4m
From Proteopedia
(Difference between revisions)
m (Protected "1j4m" [edit=sysop:move=sysop]) |
|||
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1j4m.png|left|200px]] | ||
| - | + | ==Minimized average structure of the 14-residue peptide RG-KWTY-NG-ITYE-GR (MBH12)== | |
| + | <StructureSection load='1j4m' size='340' side='right'caption='[[1j4m]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1j4m]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J4M FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1j4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4m OCA], [https://pdbe.org/1j4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j4m RCSB], [https://www.ebi.ac.uk/pdbsum/1j4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j4m ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Here we present a combinatorial approach to evolve a stable beta-hairpin fold in a linear peptide. Starting with a de novo-designed linear peptide that shows a beta-hairpin structure population of around 30%, we selected four positions to build up a combinatorial library of 20(4) sequences. Deconvolution of the library using circular dichroism reduced such a sequence complexity to 36 defined sequences. Circular dichroism and NMR of these peptides resulted in the identification of two linear 14-aa-long peptides that in plain buffered solutions showed a percentage of beta-hairpin structure higher than 70%. Our results show how combinatorial approaches can be used to obtain highly structured peptide sequences that could be used as templates in which functionality can be introduced. | ||
| - | + | Combinatorial approaches: a new tool to search for highly structured beta-hairpin peptides.,Pastor MT, Lopez de la Paz M, Lacroix E, Serrano L, Perez-Paya E Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):614-9. Epub 2002 Jan 8. PMID:11782528<ref>PMID:11782528</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1j4m" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | < | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Lacroix E]] |
| - | [[Category: | + | [[Category: Lopez de la Paz M]] |
| - | [[Category: | + | [[Category: Pastor MT]] |
| - | [[Category: | + | [[Category: Perez-Paya E]] |
| - | + | [[Category: Serrano L]] | |
| - | [[Category: | + | |
Current revision
Minimized average structure of the 14-residue peptide RG-KWTY-NG-ITYE-GR (MBH12)
| |||||||||||
