1le0: Difference between revisions
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1le1|1le1]], [[1le3|1le3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1le1|1le1]], [[1le3|1le3]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1le0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1le0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1le0 RCSB], [http://www.ebi.ac.uk/pdbsum/1le0 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1le0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1le0 OCA], [http://pdbe.org/1le0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1le0 RCSB], [http://www.ebi.ac.uk/pdbsum/1le0 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1le0" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:02, 10 September 2015
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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