Table 1 Infrared frequencies and assignment of the major infrared absorption bands in the FTIR-ATR-FPA spectra from the irradiated and control mice.
From: Long-term, non-invasive FTIR detection of low-dose ionizing radiation exposure
Peak number | Approximate absorption peak (cm–1) | Intensity (up/down), Shift (L-R) | ΔIntensity (× 10–4) | Assignment |
|---|---|---|---|---|
1 | 2922 |
| 0.3 | υas(C–H) of saturated methylene > CH2 in lipids, proteins |
2 | 2851 |
| 0.4 | υs(C–H) of saturated methylene > CH2 in lipids, proteins |
3 | 1743 |
| 0.5 | υ(C=O) of acyl groups in saturated esters like triacylglycerol |
4 | 1691 |
| 0.2 | υ(C=O) and υ(C–N) of Amide I in proteins (aide I); β-turns |
5 | 1648 |
| 1.1 | υ(C=O) and υ(C–N) of Amide I in proteins; random coils |
6 | 1626 |
| 1.5 | υ(C=O) and υ(C–N) of Amide I in proteins (aide I); β-sheets |
7 | 1553 |
| 0.9 | d(N–H) and υ(C–N) of Amide II in proteins |
8 | 1518 |
| 0.3 | Tyrosine ring stretching vibrations (–C–C/–C=C) |
9 | 1458 |
| 0.8 | δ(C–H) of CH3, CH2 in proteins, lipids |
10 | 1402 |
| 0.6 | υ(COO–) in proteins, lipids |
11 | 1336 |
| 0.3 | δ(C–H) of CH2 side chains in proteins |
12 | 1236 |
| 0.2 | υas(O–P–O) of nucleic acids, phosphorylated proteins, phospholipids |
13 | 1172 |
| 0.1 | υ(–CH2OH) coupled with δ(–C–O–) and υ(–C–O–) of the υ(–C–OH) groups of serine, threonine, and tyrosine |
14 | 1083 |
| 0.5 | υs(O–P–O) of nucleic acids, phosphorylated proteins, phospholipids |
15 | 1024 |
| 0.1 | υ(C–O) of carbohydrate side chains of proteins |
16 | 972 |
| 0.1 | trans C=C bonds |
