Table 3.
Raman modes useful in interpretation of the protein structure adapted from the works of Li-Chan [19] and Beattie et al. [3].
| Origin | Wavenumber (cm−1) | Assignment | Structural information obtained |
|---|---|---|---|
| Phenylalanine | 1006 | Breathing ring | Conformation insensitive; useful as an internal intensity standard |
| Histidine | 1409 | N-Diimidazole | Probe of ionization state, metalloprotein structure, and proton transfer in deuterated solution |
| Tryptophan | 760, 880, 1360 | Indole ring | Sharp intense band indicates buried residues; sensitive to environment polarity |
| Aspartic acid, glutamic acid | 1400–1430 | C=O stretch of COO− | Ionized carboxyl groups |
| Amide III | 1230–1240 | N-H in-plane bend, C-N stretch | Antiparallel g-sheet |
| Amide I | 1650–1660 | Amide C=O stretch, N-H wag | α-Helix |
| Aliphatic amino acids | 1450, 1465 | C-H bending | Microenvironment, polarity |