1j4m: Difference between revisions

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[[~~Image~~:~~1j4m~~.~~png~~|~~left~~|~~200px~~]]

==Minimized average structure of the 14-residue peptide RG-KWTY-NG-ITYE-GR (MBH12)==

== 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J4M FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k43|1k43]]</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=1j4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j4m RCSB], [http://www.ebi.ac.uk/pdbsum/1j4m PDBsum]</span></td></tr>

<table>

== 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.

~~{{STRUCTURE_1j4m| PDB=1j4m | SCENE= }}~~

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>

~~===Minimized average structure~~ of the ~~14-residue peptide RG-KWTY-NG-ITYE-GR (MBH12)===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_11782528}}~~

== References ==

~~==About this Structure==~~

__TOC__

~~[[1j4m]] is a 1 chain structure~~. ~~Full experimental information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=1J4M OCA].~~

</StructureSection>

==~~Reference~~==

<~~ref group="xtra">PMID:011782528<~~/~~ref~~><~~references group="xtra"~~/>

[[Category: Lacroix, E.]]

[[Category: Pastor, M T.]]

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@@ 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]], [[NMR_Ensembles_of_Models | 1 NMR models]]' 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J4M FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k43|1k43]]</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=1j4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j4m RCSB], [http://www.ebi.ac.uk/pdbsum/1j4m PDBsum]</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.
-{{STRUCTURE_1j4m|  PDB=1j4m  |  SCENE=  }}
+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>
-===Minimized average structure of the 14-residue peptide RG-KWTY-NG-ITYE-GR (MBH12)===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_11782528}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[1j4m]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4M OCA].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:011782528</ref><references group="xtra"/>
 [[Category: Lacroix, E.]]
 [[Category: Pastor, M T.]]