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.
Full text not available from this repository. (Request a copy)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 |
|---|---|
| Publication: | International Journal of Peptide and Protein Research |
| Publisher: | Munksgaard International Publishers Ltd. |
| 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.ac.in/id/eprint/33525 |
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