کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1249607 | 1495999 | 2012 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The infrared and Raman spectra of solid tridehydropeptides: Influence of ÎAla and ÎPhe on the spectral profile
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
A series of solid tripeptides Boc-Gly-X-Gly-OMe (XÂ =Â dehydroalanine (ÎAla), dehydrophenylalanine (ÎPhe)) was investigated by Raman scattering and Fourier transform infrared spectra to examine the conformational marker bands of the unsaturated residue. The observed fundamental modes gave us the opportunity to analyze structural features that change due to the substitution of Ala by ÎAla and due to the different spatial arrangement of ÎPhe (Z and E isomers). In addition, we showed the alteration of the spectral profile when the large size residue (Phe) is introduced into the backbone of the peptide with ÎPhe (in Boc-Gly-Î(Z)Phe-Phe-OMe). The frequency ranges of interest included the NH stretching, carbonyl stretching, and amide deformation modes as well as vibrations of the investigated dehydroresidues. The observed differences of positions and intensities of IR and Raman bands provided an insight into the structural and spectroscopic properties of the selected dehydropeptides.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Vibrational Spectroscopy - Volume 60, May 2012, Pages 73-78
Journal: Vibrational Spectroscopy - Volume 60, May 2012, Pages 73-78
نویسندگان
Kamilla Malek, Maciej Makowski,