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[[Image:1le0.png|left|200px]]


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==NMR structure of Tryptophan Zipper 1: a stable, monomeric beta-hairpin with a type II' turn==
The line below this paragraph, containing "STRUCTURE_1le0", creates the "Structure Box" on the page.
<StructureSection load='1le0' size='340' side='right'caption='[[1le0]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1le0]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hrw 1hrw]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LE0 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
{{STRUCTURE_1le0|  PDB=1le0  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1le0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1le0 OCA], [https://pdbe.org/1le0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1le0 RCSB], [https://www.ebi.ac.uk/pdbsum/1le0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1le0 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A structural motif, the tryptophan zipper (trpzip), greatly stabilizes the beta-hairpin conformation in short peptides. Peptides (12 or 16 aa in length) with four different turn sequences are monomeric and fold cooperatively in water, as has been observed previously for some hairpin peptides. However, the folding free energies of the trpzips exceed substantially those of all previously reported beta-hairpins and even those of some larger designed proteins. NMR structures of three of the trpzip peptides reveal exceptionally well-defined beta-hairpin conformations stabilized by cross-strand pairs of indole rings. The trpzips are the smallest peptides to adopt an unique tertiary fold without requiring metal binding, unusual amino acids, or disulfide crosslinks.


===NMR structure of Tryptophan Zipper 1: a stable, monomeric beta-hairpin with a type II' turn===
Tryptophan zippers: stable, monomeric beta -hairpins.,Cochran AG, Skelton NJ, Starovasnik MA Proc Natl Acad Sci U S A. 2001 May 8;98(10):5578-83. Epub 2001 May 1. PMID:11331745<ref>PMID:11331745</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1le0" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 11331745 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_11331745}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hrw 1hrw]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE0 OCA].
[[Category: Cochran AG]]
 
[[Category: Skelton NJ]]
==Reference==
[[Category: Starovasnik MA]]
Tryptophan zippers: stable, monomeric beta -hairpins., Cochran AG, Skelton NJ, Starovasnik MA, Proc Natl Acad Sci U S A. 2001 May 8;98(10):5578-83. Epub 2001 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11331745 11331745]
[[Category: Cochran, A G.]]
[[Category: Skelton, N J.]]
[[Category: Starovasnik, M A.]]
[[Category: Beta-hairpin]]
[[Category: Type ii' turn]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 12:56:35 2008''

Latest revision as of 21:48, 29 November 2023

NMR structure of Tryptophan Zipper 1: a stable, monomeric beta-hairpin with a type II' turnNMR structure of Tryptophan Zipper 1: a stable, monomeric beta-hairpin with a type II' turn

Structural highlights

1le0 is a 1 chain structure. This structure supersedes the now removed PDB entry 1hrw. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

A structural motif, the tryptophan zipper (trpzip), greatly stabilizes the beta-hairpin conformation in short peptides. Peptides (12 or 16 aa in length) with four different turn sequences are monomeric and fold cooperatively in water, as has been observed previously for some hairpin peptides. However, the folding free energies of the trpzips exceed substantially those of all previously reported beta-hairpins and even those of some larger designed proteins. NMR structures of three of the trpzip peptides reveal exceptionally well-defined beta-hairpin conformations stabilized by cross-strand pairs of indole rings. The trpzips are the smallest peptides to adopt an unique tertiary fold without requiring metal binding, unusual amino acids, or disulfide crosslinks.

Tryptophan zippers: stable, monomeric beta -hairpins.,Cochran AG, Skelton NJ, Starovasnik MA Proc Natl Acad Sci U S A. 2001 May 8;98(10):5578-83. Epub 2001 May 1. PMID:11331745[1]

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

References

  1. ↑ Cochran AG, Skelton NJ, Starovasnik MA. Tryptophan zippers: stable, monomeric beta -hairpins. Proc Natl Acad Sci U S A. 2001 May 8;98(10):5578-83. Epub 2001 May 1. PMID:11331745 doi:10.1073/pnas.091100898
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