Disulfide conformations in 14-membered loops investigated by Raman spectroscopy and circular dichroism

Kishore, R. ; Ishizaki, H. ; Tu, A. T. ; Ravi, A. ; Balaram, P. (1987) Disulfide conformations in 14-membered loops investigated by Raman spectroscopy and circular dichroism International Journal of Peptide & Protein Research, 30 (4). pp. 474-480. ISSN 0367-8377

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

Related URL: http://dx.doi.org/10.1111/j.1399-3011.1987.tb03355.x

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 ß-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—C αbonds. 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:Article
Source:Copyright of this article belongs to Munksgaard International Publishers.
Keywords:Circular Dichroism; Cystine Peptides; Peptide Conformation; Peptide Disulfides; Raman Spectroscopy
ID Code:91379
Deposited On:21 May 2012 08:26
Last Modified:21 May 2012 08:26

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