Role of Vibrational Spectroscopy in Stem Cell Research

Table 2

Raman spectroscopy band assignments of human cells [58].

Wavenumber (cm−1) Assignment

3070Amide B (CNH bend)
2960CH3 stretch (antisymmetric) due to methyl terminal of membrane phospholipids
2936CH3 stretch
2928CH2 antisymmetric stretch of Methylene group of membrane phospholipids
2886CH2 stretch (symmetric) due to methylene groups of membrane phospholipids
2854CH2 stretch
2739CH stretch
1736C=O stretch
1667, 1640Amide I (protein) C=O stretching of amide coupled to NH2 in-plane bending
1657, 1659C=C stretch (lipids), Amide I (α-helix, protein)
1611Tyr (aromatics)
1566Phe, Trp (phenyl, aromatics)
1550Amide II absorption due to N–H bending coupled to a C–N stretch
1509C=C stretch (aromatics)
1452CH2 stretch deformation of methylene group (lipids)
1439CH2 deformation
1420CH3 asymmetric stretching (lipids, aromatics)
1397CH3 bending due to methyl bond in the membrane
1382COO– symmetric stretching
1367CH3 symmetric stretching
1336Adenine, Phenylalanine, CH deformation
1304Lipids CH2 twist, protein amide III band, adenine, cytosine
1267Amide III (α-helix, protein)
1250Amide III (β-sheet, protein)
1235Antisymmetric phosphate stretching
1206C–C stretch, C–H bending
1165C–O stretch, COH bending
1130C–C asymmetric stretching
1100,  1094,  1081 P O 2 symmetric stretching (nucleic acids)
1065Chain C–C
1056RNA ribose C–O vibration
1003Phenylalanine (ring-breathing)
967C–C and C–N stretch P O 3 2 stretching (DNA)
957CH3 deformation (lipid, protein)
936C–C residue α-helix
921C–C stretch proline
898C–C stretch residue
870C-DNA
853Ring breathing Tyr-C–C stretch proline
828, 833Out of plane breathing Tyr; P O 2 asymmetric stretching, DNA (B-form)
807A-DNA
786DNA-RNA ( P O 2 ) symmetric stretching
746Thymine
727Adenine