1le1
From Proteopedia
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[[Image:1le1.gif|left|200px]] | [[Image:1le1.gif|left|200px]] | ||
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'''NMR Structure of Tryptophan Zipper 2: A stable, Monomeric Beta-Hairpin with a Type I' Turn''' | '''NMR Structure of Tryptophan Zipper 2: A stable, Monomeric Beta-Hairpin with a Type I' Turn''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hrx 1hrx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE1 OCA]. | |
==Reference== | ==Reference== | ||
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] | 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: Protein complex]] | ||
[[Category: Cochran, A G.]] | [[Category: Cochran, A G.]] | ||
[[Category: Skelton, N J.]] | [[Category: Skelton, N J.]] | ||
[[Category: Starovasnik, M A.]] | [[Category: Starovasnik, M A.]] | ||
| - | [[Category: | + | [[Category: Beta-hairpin]] |
| - | [[Category: | + | [[Category: Type i' turn]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:49:55 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:49, 2 May 2008
NMR Structure of Tryptophan Zipper 2: A stable, Monomeric Beta-Hairpin with a Type I' Turn
Overview
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.
About this Structure
This structure supersedes the now removed PDB entry 1hrx. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 23:49:55 2008
