Table 1.
Major band assignments in ex vivo porcine skin Raman spectra.
| Band positions (cm−1) | Assignments | Structure | Reference values (cm−1) |
|---|---|---|---|
| 813 |
ν(C–C) ν(C–O–C) |
Protein backbone, collagen cross-link, proline, hydroxyproline, tyrosine | 813–8176,7,29 |
| 853 | ν(C–C) | Proline, hydroxyproline, tyrosine | 853–8566,7,29 |
| 873 | ν(C–C) | Hydroxyproline, tryptophan, protein | 873–8796,7,29 |
| 919 | ν(C–C) | Proline | 919–9206,7,29 |
| 937 | ν(C–C) | Protein (collagen), α-helix, proline, hydroxyproline | 933–9386,7,29 |
| 1002 | ν(C–C) | Phenylalanine (collagen), protein | 1000–10056,7,29 |
| 1030 | ν(C–C), δ(C–H), ν(C–N), δ(CH2CH3) | Phenylalanine (collagen), lipids, proteins | 1030–10346,29 |
| 1247 | ν(C–N), δ(N–H) | Amide III, proteins | 1242–12557,29 |
| 1270 | ν(C–N), δ(N–H) | Amide III (collagen), α-helix | 1270–12807,29,38 |
| 1317 | δ(CH3CH2) | Collagen, nuclei acids | 132229 |
| 1342 | δ(C–H), δ(CH3CH2) | Collagen, protein, lipids | 1330–13407,29 |
| 1448 | δ(CH2), δ(CH2CH3) | Collagen, protein, lipids | 1440–14507,29 |
| 1662 | ν(C=O), ν(C=C), ν(C–N), δ(N–H) | Amide I (collagen) | 1650–16767,29 |
Abbreviations: ν, stretching mode; δ, in-plane bending mode.