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. Author manuscript; available in PMC: 2019 Jun 21.
Published in final edited form as: J Biophotonics. 2017 Sep 12;11(3):10.1002/jbio.201700057. doi: 10.1002/jbio.201700057

TABLE 1.

List of Gaussian oscillators used to fit the experimental absorbance curve with the individual assignments [10, 23] based on a majority absorbance contribution

Oscillator number Wave number (cm−1) Assignment
1 1735 Lipids: Symmetric vibration C=O
2 1680 β (antiparallel + turn): Amide I of proteins
3 1653 α-helix structures: Amide I of proteins
4 1632 β-pleated sheet structures: Amide I of proteins
5 1618 Side chain: Amide I of proteins
6 1588 C—C stretching of phenyl rings: Amide II of proteins
7 1555 β-pleated sheet structures: Amide II of proteins
8 1529 C=N adenine, cytosine, guanine: Amide II of proteins
9 1500 C—H bending of phenyl rings
10 1450 Lipids: CH2 symmetric, proteins: CH3 asymmetric deformation
11 1395 Amino acid: Symmetric stretching of COO-, proteins: CH3
12 1350 Adenine: Stretch carboxyl group COO
13 1300 Amide III: C—H/N—H deformation vibrational modes methyl group
14 1245 Lipid phosphates, DNA, RNA: Asymmetric (PO2−) stretching
15 1155 C—O stretching vibrations
16 1116 Symmetrical stretching P—O—C, C—O(H) stretching bands of RNA
17 1076 Mannose: C—O stretching (carbohydrate α-anomer)
18 1033 Glucose: C—O stretching (carbohydrate, β-anomer)