1j4m: Difference between revisions
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==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: Lacroix | <div class="pdbe-citations 1j4m" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Perez-Paya | __TOC__ | ||
[[Category: Serrano | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Lacroix E]] | |||
[[Category: Lopez de la Paz M]] | |||
[[Category: Pastor MT]] | |||
[[Category: Perez-Paya E]] | |||
[[Category: Serrano L]] | |||
Latest revision as of 18:42, 29 November 2023
Minimized average structure of the 14-residue peptide RG-KWTY-NG-ITYE-GR (MBH12)
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