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Conformations of dehydrophenylalanine containing peptides. NMR studies on three tripeptides with a central dehydrophenylalanyl residue.

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.
Official URL: http://onlinelibrary.wiley.com/doi/10.1111/j.1399-...

Abstract

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
URI: http://eprints.iisc.ernet.in/id/eprint/33522

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