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. 2021 Apr 1;10(7):1405. doi: 10.3390/jcm10071405

Table 3.

μ-RS, SERS, and FT-IR spectroscopy peak position and assignments for GCF samples References [24,25,26,27,39].

Assignment Mode Peak Position
SERS (cm−1)
Peak Position
Raman (cm−1)
Peak Position
FT-IR (cm−1)
0 2 7 14 0 2 7 14 0 2 7 14
S–S bond
stretching
465
Phenylalanine 621
Tyrosine 825
Deoxyribose bending CO2H of tyrosine 895 897
PO43− 946
PO43− ν1 symmetric stretching, apatite 984 985 986 986
C–H bending
phenylalanine
1007 1002
C–O stretching of carbohydrates 1039 1038 1035 1039
symmetric PO2
stretching of nucleic acids
1087 1087 1067 1092
Nucleic acid base PO2 1100 1100
C–O asymmetric stretching and COH bending
of lipids
1160 1158 1158 1158
Cytochrome 1167 1167 1167
Nucleic acid
C–N
1176 1176
Amide III 1242 1242 1242
PO2 asymmetric stretching of
nucleic acids
1253 1255 1254 1253
Amide III, CH2 deformation 1276 1280
CH2/CH3 twisted 1311 1314 1313 1308
Adenine/guanine of nucleic acids 1348 1348 1348 1345 1345 1345
symmetric bending of CH3 of
nucleic acids
1376 1361 1388 1384
Cytochrome 1390
COO– stretching of aminoacids 1424 1419 1415 1423
CH3 symmetric stretching CH2
lipids/proteins
scissoring
1462 1459
CH2 1470
Carotene 1540 1540
Amide II (N–H bending of proteins) 1547 1539 1545 1548
Amide II/cytochrome 1577 1575 1577 1577 1577
C=C stretching of amino acids 1598 1594 1598 1596
Amide I
(β-sheet)
1625 1625 1611
Amide I (α-helix) 1641 1640 1640
C=O stretching of proteins (Amide I band) 1656 1650 1655 1655
CH3 symmetric stretching
of lipids
2873 2880 2877 2881
CH2 asymmetric stretching of lipids 2927 2930 2929 2916
CH3 asymmetric stretching of lipids 2974 2981 2984 2937
NH stretching of Amide A OH stretching 3356 3357 3359 3365