Raghothama, Srinivasa Rao and Awasthi, Satish Kumar and Balaram, Padmanabhan (1998) Beta-Hairpin nucleation by Pro-Gly beta-turns. Comparison of D-Pro-Gly and L-Pro-Gly sequences in an apolar octapeptide. In: Journal of Chemical Society, Perkin Transactions 2 (2). pp. 137-144.
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The solution conformation of the synthetic octapeptide Boc-Leu-Val-Val-D-Pro-Gly-Leu-Val-Val-OMe 1 and Boc-Leu-Val-Val-Pro-Gly-Leu-Val-Val-OMe 2 have been investigated in organic solvents by NMR spectroscopy. Peptide 1 adopts well-defined beta-hairpin conformations in CDCl3, C6D6 and (CD3)2SO, nucleated by a D-Pro-Gly Type II9 beta-turn, as demonstrated by the observation of characteristic nuclear Overhauser effects (NOEs) between backbone protons and solvent shielding of NH groups involved in cross-strand hydrogen bonding. Chemical shifts and coupling constants provide further support for the beta-hairpin conformation, which is consistent with the observation of a single negative circular dichroism band at 216 nm in methanol. In peptide 2, there is no characteristic interstrand NOE observed in (CD3)2SO, while in CDCl3 pronounced aggregation results in line broadening. The observation of a low temperature coefficient for the Leu(6)NH proton favours a population of Pro-Gly Type II beta-turn conformations. These results suggest that in short peptide sequences, the precise nature of the beta-turn is critical for hairpin formation, with Type II9 beta-turns being particularly effective.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to the Royal Society of Chemistry.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit
Division of Chemical Sciences > Sophisticated Instruments Facility
|Date Deposited:||06 Oct 2004|
|Last Modified:||19 Sep 2010 04:16|
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