Venkatraman, Janani and Gowda, Nagana GA and Balaram, Padmanabhan (2002) Design and Construction of an Open Multistranded ‚beta-Sheet Polypeptide Stabilized by a Disulfide Bridge. In: Journal of the American Chemical Society, 124 (18). pp. 4987-4994.
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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 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.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to American Chemical Society|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit
Division of Chemical Sciences > Sophisticated Instruments Facility
|Date Deposited:||28 Aug 2004|
|Last Modified:||19 Sep 2010 04:14|
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