1le0: Difference between revisions
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==NMR structure of Tryptophan Zipper 1: a stable, monomeric beta-hairpin with a type II' turn== | ==NMR structure of Tryptophan Zipper 1: a stable, monomeric beta-hairpin with a type II' turn== | ||
<StructureSection load='1le0' size='340' side='right' caption='[[1le0 | <StructureSection load='1le0' size='340' side='right'caption='[[1le0]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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 [ | <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> | ||
</td></tr><tr id=' | </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=' | <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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Cochran AG]] | ||
[[Category: | [[Category: Skelton NJ]] | ||
[[Category: | [[Category: Starovasnik MA]] | ||
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
Publication Abstract from PubMedA 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
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