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1jy4
From Proteopedia
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[[Image:1jy4.jpg|left|200px]] | [[Image:1jy4.jpg|left|200px]] | ||
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'''B4DIMER: A DE NOVO DESIGNED EIGHT-STRANDED BETA-SHEET ASSEMBLED USING A DISULFIDE BOND''' | '''B4DIMER: A DE NOVO DESIGNED EIGHT-STRANDED BETA-SHEET ASSEMBLED USING A DISULFIDE BOND''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JY4 OCA]. | |
==Reference== | ==Reference== | ||
Design and construction of an open multistranded beta-sheet polypeptide stabilized by a disulfide bridge., Venkatraman J, Nagana Gowda GA, Balaram P, J Am Chem Soc. 2002 May 8;124(18):4987-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11982362 11982362] | Design and construction of an open multistranded beta-sheet polypeptide stabilized by a disulfide bridge., Venkatraman J, Nagana Gowda GA, Balaram P, J Am Chem Soc. 2002 May 8;124(18):4987-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11982362 11982362] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Balaram, P.]] | [[Category: Balaram, P.]] | ||
[[Category: Gowda, G A.Nagana.]] | [[Category: Gowda, G A.Nagana.]] | ||
[[Category: Venkatraman, J.]] | [[Category: Venkatraman, J.]] | ||
| - | [[Category: | + | [[Category: De novo protein design]] |
| - | [[Category: | + | [[Category: Disulfide bond]] |
| - | [[Category: | + | [[Category: Eight-stranded beta-sheet]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:03:54 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:03, 2 May 2008
B4DIMER: A DE NOVO DESIGNED EIGHT-STRANDED BETA-SHEET ASSEMBLED USING A DISULFIDE BOND
Overview
The design and characterization of an open eight-stranded beta-sheet in a synthetic, 2-fold symmetric 70-residue peptide is described. The design strategy involves the generation of a 35-residue four-stranded beta-sheet peptide in which successive hairpins are nucleated by appropriately positioned (D)Pro-Xxx sequences. Oxidative dimerization using a single Cys residue positioned at the center of the C-terminal strand results in a disulfide-bridged eight-stranded structure. Nuclear Overhauser effects firmly establish an eight-stranded beta-sheet in methanol. In water, the outer strands are frayed, but a well-defined four-stranded beta-sheet stabilized by a disulfide bridge and a hydrophobic cluster is determined from NMR data. Comparison of the precursor peptide with the disulfide-bridged dimer reveals considerable enhancement of beta-sheet content in the latter, suggesting that the disulfide cross-link is an effective strategy for the stabilization of beta-sheets.
About this Structure
Full crystallographic information is available from OCA.
Reference
Design and construction of an open multistranded beta-sheet polypeptide stabilized by a disulfide bridge., Venkatraman J, Nagana Gowda GA, Balaram P, J Am Chem Soc. 2002 May 8;124(18):4987-94. PMID:11982362 Page seeded by OCA on Fri May 2 22:03:54 2008
