Table 1.
Peak assignment of the Raman spectra of human hair fibre and pure keratin
| Raman shift (cm−1) | Bands assignments | |
|---|---|---|
| Human Hair | Pure keratin | |
| 415 | (NCC) Ala | |
| 510 | 510 | Disulfide Cys (S‐S) strech |
| 581 | Disulfide Cys (S‐S) strech and Cys residues | |
| 643 | 643 | Tyr |
| 746 | 748 | Trp |
| 851 | 851 | Ring breathig mode of Tyr |
| 894 | 886 | Trp |
| 934 | 934 | Stretch C‐C skeletal a‐helix |
| 958 | CH3, CCH olefinic, CH2 rock | |
| 1000 | 1000 | Symmetric ring breathing of Phe |
| 1041 | 1041 | CH inplane bending of Phe |
| 1060 | CC skeletal, trans conformation | |
| 1126 | 1126 | CC skeletal, trans conformation, C‐N stretch |
| 1177 | 1177 | Tyr |
| 1245 | 1245 | Amide III (unordered) |
| 1316 | 1301 | CH2 |
| 1339 | CH2 bend, Trp | |
| 1449 | 1449 | CH2 bending mode |
| 1553 | Trp | |
| 1614 | 1614 | Tyr and Trp |
| 1656 | 1656 | C=O Amide I |
| 2852 | CH stretchnig (CH2, CH3) | |
| 2874 | 2883 | CH stretchnig (CH2, CH3) |
| 2935 | 2935 | CH stretchnig (CH2, CH3) |