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Cystine peptides. Disulfide conformations in fourteen membered loops investigated by Raman spectroscopy and circular dichroism

Kishore, R and Ishizaki, H and Tu, AT and Ravi , A and Balaram, Padmanabhan (1987) Cystine peptides. Disulfide conformations in fourteen membered loops investigated by Raman spectroscopy and circular dichroism. In: International Journal of Peptide and Protein Research, 30 (4). pp. 474-480.

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

Abstract

NHCH3 (X = Gly 1, Ala 2, Aib 3, Leu 4 and D-Ala 5), have been investigated by Raman and circular dichroism (CD) spectroscopy. Solid state Raman spectra are consistent with β-turn conformations in all five peptides. These peptides exhibit similar conformations of the disulfide segment in the solid state with a characteristic disulfide stretching frequency at 519 ± 3 cm-1, indicative of a trans-gauche-gauche arrangement about the Cα—Cβ—S—S—Cβ—Cα bonds. The results correlate well with the solid state conformations determined by X-ray diffraction for peptides 3 and 4. CD studies in chloroform and dimethylsulfoxide establish solvent dependent conformational changes for peptides 1, 3 and 5. Disulfide chirality has been derived using the quadrant rule. CD results together with previously reported nuclear magnetic resonance (n.m.r.) data suggest a conformational coupling between the peptide backbone and the disulfide segment

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Munksgaard International Publishers Ltd.
Keywords: Circular dichroism; cystine peptides; peptide conformation; peptide disulfides; Raman spectroscopy.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 29 Oct 2010 07:41
Last Modified: 29 Oct 2010 07:41
URI: http://eprints.iisc.ernet.in/id/eprint/33525

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