Chauhan, VS and Sharma, AK and Uma, K and Paul, PKC and Balaram, Padmanabhan (1987) Conformations of dehydrophenylalanine containing peptides. NMR studies on three tripeptides with a central dehydrophenylalanyl residue. In: International Journal of Peptide and Protein Research, 29 (1). pp. 126-133.Full text not available from this repository.
Three tripeptides containing a central Z-dehydrophenylalanine residue (Δz-Phe), Boc-L-Phe-Δz-Phe-X-OMe (X = L-Val 1, L-Leu 2 and X = L-Ala 3) have been synthesized and their solution conformations investigated by 270 MHz 1H NMR spectroscopy. In all three peptides, conformations involving the X residue NH in an intramolecular hydrogen bond were favoured in CDCl3 solutions. Studies of the nuclear Overhauser effect (NOE) provided support for a Type II β turn conformation in these peptides with Phe and Δz-Phe occupying the i + 1 and i + 2 positions, respectively. Significantly different conformations lacking any intramolecular hydrogen bonds were observed for peptide 1 in (CD3)2SO. NOE results were consistent with a significant population of molecules having semi-extended conformations (ø > 100°) at the Δz-Phe residue.
|Item Type:||Journal Article|
|Additional Information:||copyright of this article belongs to John Wiley & Sons.|
|Keywords:||dehydrophenylalanine peptides; β turns; nuclear Overhauser effects.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||29 Oct 2010 07:49|
|Last Modified:||29 Oct 2010 07:49|
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