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1j4m
From Proteopedia
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| - | [[Image:1j4m.jpg|left|200px]]<br /><applet load="1j4m" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1j4m" /> | ||
| - | '''Minimized average structure of the 14-residue peptide RG-KWTY-NG-ITYE-GR (MBH12)'''<br /> | ||
| - | == | + | ==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. | 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> | |
| - | [[Category: | + | <div class="pdbe-citations 1j4m" style="background-color:#fffaf0;"></div> |
| - | [[Category: Lacroix | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: Perez-Paya | + | </StructureSection> |
| - | [[Category: Serrano | + | [[Category: Large Structures]] |
| - | + | [[Category: Lacroix E]] | |
| - | + | [[Category: Lopez de la Paz M]] | |
| - | + | [[Category: Pastor MT]] | |
| + | [[Category: Perez-Paya E]] | ||
| + | [[Category: Serrano L]] | ||
Current revision
Minimized average structure of the 14-residue peptide RG-KWTY-NG-ITYE-GR (MBH12)
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