FTIR and Raman Characteristic Peak Frequencies in Biological Studies - Vibrational Spectroscopy for Tissue Analysis - page 222

Table 8.1 ( Continued )
Major Characteristic Peak Frequencies Reported in the Literature

Reference
Number Peak Assignment FT-IR Raman

ν(C-C), proline + δ(CCH) ring
breathing, tyrosine (protein
assignment and polysaccharide)

* 20

δ(CCH) phenylalanine, olefinic
(protein assignment and
polysaccharide)

* 33

855/6 cm −1 Proline, hydroxyproline, tyrosine * 3

C-C stretching, proline (collagen
assignment)

* 19

856 cm −1 Amino acid side chain vibrations

of proline and hydroxyproline,
as well as a (C-C) vibration of
the collagen backbone
hydroxyproline (collagen type I)

* 3

857 cm −1 CH 2, 6 out-of-plane bending * 6

859 cm −1 Tyrosine, collagen * 9

860 cm −1 C 3 ' endo/anti (A-form helix)

conformation

* 23

Phosphate group * 2

Phosphatidic acid * 2

864 cm −1 Structural proteins like collagen * 34

865 cm −1 Ring deformation, OC-N and

cyclic C-C-C stretch

* 14

867 cm −1 Ribose vibration, one of the

distinct RNA modes (with 915
and 974 cm −1 )

* 12

868 cm −1 Left-handed helix DNA ( Z form) * * 23

C-C stretching, hypro (collagen
assignment)

* 19

Monosaccharides (β-fructose),
(C-O-C) skeletal mode

* 7

Disaccharide (sucrose), (C-O-C)
skeletal mode

* 7

Polysaccharides, amylose * 7

Polysaccharides, amylopectin * 7

Proline * 17

869 cm −1 Proline * 9

870 cm −1 Most probably due to single-bond

stretching vibrations for the
amino acids proline and valine
and polysaccharides

* 29

C-C stretching, hypro (collagen
assignment)

* 19

Proline * 17