Das, C. ; Balaram, P. ; Nayak, V. ; Raghothama, S. (2000) Synthetic protein design: construction of a four-stranded β-sheet structure and evaluation of its integrity in methanol-water systems The Journal of Peptide Research, 56 (5). pp. 307-317. ISSN 1397-002X
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Official URL: http://www3.interscience.wiley.com/journal/1201004...
Related URL: http://dx.doi.org/10.1034/j.1399-3011.2000.00775.x
Abstract
The characterization of a four-stranded β-sheet structure in a designed 26-residue peptide Beta-4 is described. The sequence of Beta-4 (Arg-Gly-Thr-Ile-Lys-Dpro-Gly-Ile-Thr-Phe-Ala-DPro-Ala-Thr-Val-Leu-Phe-Ala-Val-DPro-Gly-Lys-Thr-Leu-Tyr-Arg) was chosen such that three strategically positioned DPro-Xxx segments nucleate type II'β-turns, which facilitate hairpin extension. A four-stranded β-sheet structure is determined in methanol from 500 MHz 1H NMR data using a total of 100 observed NOEs, 11 dihedral restraints obtained from vicinal JCαH-NH values and 10 hydrogen bonding constraints obtained from H/D exchange data. The observed NOEs provide strong evidence for a stable four-stranded sheet and a nonpolar cluster involving Ile8, Phe10, Val15 and Phe17. Circular dichroism studies in water-methanol mixtures provide evidence for melting of the β-sheet structure at high water concentrations. NMR analysis establishes that the four-stranded sheet in Beta-4 is appreciably populated in 50% (v/v) aqueous methanol. In water, the peptide structure is disorganized, although the three β-turn nuclei appear to be maintained.
Item Type: | Article |
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Source: | Copyright of this article belongs to John Wiley and Sons, Inc. |
Keywords: | Protein Design; Designed β-sheet Motif; Synthetic Peptide; Conformational Analysis; NMR |
ID Code: | 4541 |
Deposited On: | 18 Oct 2010 07:34 |
Last Modified: | 16 May 2016 15:10 |
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