Table 4.
Peak positions and tentative assignments of the major Raman bands from biological samples.
| Peak position, cm−1 | Major Assignments |
|---|---|
| 826[39] | O-P-O stretch DNA |
| 853[40] | Ring breathing mode of tyrosine and C-C stretch of proline ring |
| 875[41] | Antisymmetric stretch vibration of choline group N + (CH3)3, characteristic for phospholipids Phosphatidylcholine, sphingomyelin |
| 928[42] | ν(C-C), stretching-probably in amino acids proline & valine (protein band) |
| 970[43] | Phosphate monoester groups of phosphorylated proteins & cellular nucleic acids |
| 1000[44] | Phenylalanine Bound & free NADH |
| 1030[45] | Phenylalanine of collagen |
| 1096[46] | O-P-O (stretching PO2) symmetric (Phosphate II) of phosphodiesters |
| 1122[47] | νsym(C-O-C) (polysaccharides, cellulose) |
| 1172[48] | δ(C-H), tyrosine (protein assignment) |
| 1246[45] | Amide III (of collagen) |
| 1310[49] | CH3CH2 twisting mode of collagen/lipids |
| 1330[44], [50], [51] | Typical phospholipids Region associated with DNA & phospholipids Collagen Nucleic acids and phosphates |
| 1447[52] | CH2 bending mode of proteins. CH2 (overlapping) asymmetric CH3 bending, and CH2 scissoring (associated with elastin, collagen, and phospholipids) |
| 1575[53] | Ring breathing modes in the DNA bases G, A (ring breathing modes of the DNA/RNA bases) |
| 1656[52] | Amide I (C = O stretching mode of proteins, a-helix conformation)/C = C lipid stretch |