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. 2012 Nov 15;17(11):116021. doi: 10.1117/1.JBO.17.11.116021

Table 1.

Raman band frequencies and assignments of Brain Tissue.

Raman shift cm1 Assignmenta Attribution remarks
676 ν (δ (CCN), Vinyl & Porphyrin CYTc, G of DNA
754 CH2 Rock, Sym. breathing Tryp, mitochondria 2nd peak 747  cm1, CYT.c
973 CH out of plane deformation CC Asym. Str. deoxygenated of cells porphyrin macrocycle
1004 Symmetric CC aromatic ring breathing Phenylalanine, Collagen IV, I
1088 CC stretch, CC skeletal stretch trans, PO2 symmetric Protein, phospholipid, glycogen Collagen IV, I
1128 CC stretching, trans Lipids
1156 CC stretch β-carotene
1173 CH in-plane bending Tyrosine, hemoglobin, Flavin
1214 >(1200–1300) Amide III Homo polypeptide
1301 Amide III, δ (NH)-30%, α-helix, ν (CN)-40% & δ(CH3) δ and ν Coupled in-phase, Collagen IV, I
1338 CH2 Deformation Protein, A and G of DNA/RNA
1358 CH3(CO), Trp., mitochondria, CYTc
1378 CH3 in-phase deformation T, A, G of DNA
1428–1471 δ (CN) bending, δ(CH)3 out-of-phase deformation Lipid, protein
1527 (1500–1600) Amide II, Shift to 1548, (CC) stretch parallel β-sheet, protein, tryp., carotenoid (1532  cm1 in cancer)
1548 Amide II, in plane δ (NH) bending: 60%; ν (CN):40%; Trp, cytochrome c, δ and ν coupled out-of-phase, NADH
1587 CC stretching, CH bending Trp, mitochondria, NADH
1605 CO stretching, CC bending Phe., tyr.
1639 Amide I in α-helix protein
1667 Amide I, β-sheet, ν (CO) 80% Salt environment effect, Unordered or random structure, Collagen IV, I
1732 ν (CC) Lipids, phospholipids
2727 1378  cm1 bend overtone  
2850 ν(CH2) Poly methylene chain, F
2891 ν (CH2, FR) Poly methylene chain
2934 ν (CH3, FR) P.F.
3060 CH3(CO)  
3104 ν(OH) water band  
3156 ν(OH) water band  
3288 OH, Liquid water  
3444 OH, Liquid water  
a

Refs: [20, 21, 24, 30, 31, 33, 34, 35]; ν: stretch; FR: Fermi resonance; δ: bending; sym.: symmetric, trp.: tryptophan, CYTc: cytochrome c; P: protein; F: fat.