Awasthi, Satish Kumar and Raghothama, Srinivasa Rao and Balaram, Padmanabhan (1996) Conformational variability in short acyclic peptides. Stabilization of multiple beta-turn structures in organic solvents. In: Journal of the Chemical Society, Perkin Transactions 2 (12). pp. 2701-2706.
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The conformational characteristics of three hexapeptides Boc-Leu-Xxx-Val-Leu-Aib-Val-OMe(Xxx = Ala 1, D-Ala2, Gly 3; Aib =alpha-aminoisobutyryl) have been probed in CDCl3 solution by NMR methods using solvent perturbation of chemical shifts and radical broadening of NH resonances to delineate intramolecularly hydrogen bonded NH groups. Nuclear Overhauser effects (NOEs) provide additional information on preferred backbone conformations. The substituent at position 2 acts as a major conformational determinant. While a continuous 310 helical conformation is favoured for the peptide with Xxx = Ala, a multiple beta-turns conformation is supported by both NMR and CD data for the peptide with Xxx =D-Ala. In the peptide with Xxx = Gly CD and NMR data suggest that both 310 helical and multiple turns conformations are simultaneously populated. The results suggest that incorporation of D-amino acids and Aib residues into all L-sequences may prove useful in generating sequences containing multiple turns.
|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|
|Date Deposited:||28 Oct 2004|
|Last Modified:||17 Jan 2012 06:23|
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