1le1

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{{STRUCTURE_1le1| PDB=1le1 | SCENE= }}
{{STRUCTURE_1le1| PDB=1le1 | SCENE= }}
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'''NMR Structure of Tryptophan Zipper 2: A stable, Monomeric Beta-Hairpin with a Type I' Turn'''
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===NMR Structure of Tryptophan Zipper 2: A stable, Monomeric Beta-Hairpin with a Type I' Turn===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11331745 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11331745}}
==About this Structure==
==About this Structure==
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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].
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This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hrx 1hrx]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE1 OCA].
==Reference==
==Reference==
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[[Category: Beta-hairpin]]
[[Category: Beta-hairpin]]
[[Category: Type i' turn]]
[[Category: Type i' turn]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:49:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:57:12 2008''

Revision as of 09:57, 2 July 2008

Image:1le1.png

Template:STRUCTURE 1le1

NMR Structure of Tryptophan Zipper 2: A stable, Monomeric Beta-Hairpin with a Type I' Turn

Template:ABSTRACT PUBMED 11331745

About this Structure

This structure supersedes the now removed PDB entry 1hrx. Full experimental 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 Wed Jul 2 12:57:12 2008

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