1jy6

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(New page: 200px<br /><applet load="1jy6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jy6" /> '''B4DIMERA: A DE NOVO DESIGNED FOUR-STRANDED B...)
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[[Image:1jy6.gif|left|200px]]<br /><applet load="1jy6" size="350" color="white" frame="true" align="right" spinBox="true"
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'''B4DIMERA: A DE NOVO DESIGNED FOUR-STRANDED BETA-SHEET ASSEMBLED USING A DISULFIDE BOND'''<br />
'''B4DIMERA: A DE NOVO DESIGNED FOUR-STRANDED BETA-SHEET ASSEMBLED USING A DISULFIDE BOND'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1JY6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JY6 OCA].
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1JY6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JY6 OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Balaram, P.]]
[[Category: Balaram, P.]]
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[[Category: Gowda, G.A.Nagana.]]
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[[Category: Gowda, G A.Nagana.]]
[[Category: Venkatraman, J.]]
[[Category: Venkatraman, J.]]
[[Category: de novo protein design]]
[[Category: de novo protein design]]
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[[Category: four-stranded beta-sheet]]
[[Category: four-stranded beta-sheet]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:25:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:01 2008''

Revision as of 11:28, 21 February 2008


1jy6

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B4DIMERA: A DE NOVO DESIGNED FOUR-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

1JY6 is a Protein complex structure of sequences from [1]. 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

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