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. 2008 Nov 4;99(11):1859–1866. doi: 10.1038/sj.bjc.6604753

Table 4. Major spectral peaks responsible for the 2-band discrimination and proposed biomolecular assignments for discriminant function 1.

Direction Wavenumber (cm−1) Proposed biomolecular assignment
+ve 1068 C-O stretch, deoxyribose/ribose, DNA, RNA
+ve 1265 Amide III (NH bend (55%), C-C stretch (19%), C-N stretch (15%), CO bend (11%)) or PO2− stretch, RNA, DNA
+ve 1415 C-N stretch, N-H, C-H deformation
+ve 1541 Amide II of α-helical structures (NH bend (43%), C-N stretch (29%), CO bend (15%), C-C stretch (9%), N-C stretch (8%))
+ve 1641 Amide I (C-O stretch (76%), C-N stretch (14%), CCN deformation (10%))
+ve 1645 Amide I (C-O stretch (76%), C-N stretch (14%), CCN deformation (10%))
+ve 1672 Amide I of turns structure (C-O stretch (76%), C-N stretch (14%), CCN deformation (10%))
+ve 2910 C-H stretch (asymmetric) of >CH2 in fatty acids, lipids, proteins
−ve 1244 Amide III (NH bend (55%), C-C stretch (19%), C-N stretch (15%), CO bend (11%))
−ve 1290 Amide III (NH bend (55%), C-C stretch (19%), C-N stretch (15%), CO bend (11%))
−ve 1364 Amide III (NH bend (55%), C-C stretch (19%), C-N stretch (15%), CO bend (11%))
−ve 1558 Amide II (NH bend (43%), C-N stretch (29%), CO bend (15%), C-C stretch (9%), N-C stretch (8%))
−ve 1655 Amide I of α-helical (C-O stretch (76%), C-N stretch (14%), CCN deformation (10%))
−ve 1683 Amide I of turns or antiparallel β-sheet structures (C-O stretch (76%), C-N stretch (14%), CCN deformation (10%))
−ve 1718 C-O stretch of carbonic acid
−ve 2850 C-H symmetric stretch of –CH2 in fatty acids, lipids and proteins
−ve 2918 C-H stretch (asymmetric) of >CH2 in fatty acids, lipids and proteins
−ve 2955 C-H antisymmetric stretch of –CH3 in fatty acids, lipids and proteins