Table 2 Assignments for the main vibrational bands of micro-FTIR blood serum (Fig. 2a).
Wavenumber (cm\(^{-1}\)) | Assignment | References |
|---|---|---|
840–845 | Left-handed helix DNA (Z form) | |
850–856 | \(\hbox {C}_{2}^{'}\) endo/anti of deoxyribose in B-form helix conformation | |
886 | C–C, C–O deoxyribose | |
930 | Left-handed helix DNA (Z form) | |
1030 | Stretching C–O ribose | |
1080 | Ring stretching vibrations in phenylalanine, tryptophan or tyrosine | |
1120 | Symmetric stretching P–O–C, phosphorylated saccharide residue | |
1165 | C–O stretching mode of C–OH groups of serine, threonine, tyrosine | |
1245 | Amide III \(\alpha \)-helix conformation of proteins | |
1315 | Amide III of proteins | |
1350 | Stretching C–O, deformation C–H, deformation N–H | |
1400 | Symmetric stretching vibration of COO– group of fatty acids and amino acids | |
1440 | Stretching C–H in polysaccharides, pectin | |
1450 | Asymmetric \(\hbox {CH}_3\) bending in proteins | |
1470 | \(\hbox {CH}_{2}\) bending vibration in lipids and proteins | |
1500 | In-plane CH bending vibration from the phenyl ring in phenylalanine, tryptophan or tyrosine | |
1515–1580 | Amide II of proteins | |
1630–1665 | \(\beta \)-sheet structure of Amide I of proteins | |
1683 | Unordered random coils and turns of Amide I of proteins | |
1689–1698 | \(\beta \)-sheet structure of Amide I of proteins | |
1700–1708 | C=O in thymine | |
1735 | C=O in polysaccharides; new COO– group vibration due to glycated human serum albumin | |
1768–1786 | methyl-esterified C=O vibration in IgG COO– group—glycosilation (IgG with sialylate N-glycans) |
