Gupta, Alka ; Mehrotra, Ranjana ; Klimov, Evgueni ; Siesler, Heinz Wilhelm ; Joshi, Ratanmani M. ; Chauhan, Virander Singh (2006) Thermal stability of dehydrophenylalanine-containing model peptides as probed by infrared spectroscopy: a case study of α-helical and a 310- helical peptide Chemistry and Biodiversity, 3 (3). pp. 284-295. ISSN 1612-1872
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Official URL: http://onlinelibrary.wiley.com/doi/10.1002/cbdv.20...
Related URL: http://dx.doi.org/10.1002/cbdv.200690031
Abstract
The temperature-dependent secondary-structural changes in the two known helical model peptides Boc-Val-ΔPhe-Ala-Leu-Gly-OMe (1; α-helical) and Boc-Leu-Phe-Ala-ΔPhe-Leu-OMe (2; 310-helical), which both comprise a single dehydrophenylalanine (ΔPhe) residue, were investigated by means of FT-IR spectroscopy (peptide film on KBr). Both the first-order and the better-resolved second-order derivative IR spectra of 1 and 2 were analyzed. The ν(NH) (3240-3340 cm-1), the Amide-I (1600-1700 cm-1), and the Amide-II (1510-1580 cm-1) regions of 1 and 2 showed significant differences in thermal-denaturation experiments (22°→144°), with the 310-helical peptide (2) being considerably more stable. This observation was rationalized by different patterns and strengths of intramolecular H-bonds, and was qualitatively related to the different geometries of the peptides. Also, a fair degree of residual secondary-structural elements were found even in the 'denatured' states above 104° (1) or 134° (2).
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to John Wiley and Sons. |
| Keywords: | Amino Acids; Peptides; Thermal Denaturation; IR Spectroscopy; Dehydroamino Acids |
| ID Code: | 77434 |
| Deposited On: | 12 Jan 2012 11:35 |
| Last Modified: | 12 Jan 2012 11:35 |
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