Biomedical Engineering Reference
In-Depth Information
Table 8.1 ( Continued )
Major Characteristic Peak Frequencies Reported in the Literature
Reference
Number
Peak
Assignment
FT-IR
Raman
932 cm −1
Skeletal C-C, α-helix
*
9
933 cm −1
Proline, hydroxyproline, ν(C-C)
skeletal of collagen backbone
*
3
934 cm −1
C-C backbone (collagen
assignment)
*
19
935 cm −1
C-C stretching mode of proline,
valine, and protein backbone
*
10, 20
(α-helix conformation)/glycogen
(protein assignment)
*
9
Ρ(CH 3 ) terminal, proline, valine +
ν(CC) α-helix keratin (protein
assignment)
*
33
936 cm −1
Protein peak
*
17
937 cm −1
Proline (collagen type I)
*
3
Amino acid side chain vibrations
of proline and hydroxyproline,
as well as a
*
3
(C-C) vibration of the collagen
backbone
C-C backbone (collagen
assignment)
*
19
Glycogen
*
8
ν(C-C) residues (α-helix)
*
43
Out-of-phase ring CH wag
*
14
937/8 cm −1
Proline, hydroxyproline, ν(C-C)
skeletal of collagen backbone
*
3
938 cm −1
Unassigned
*
38
C-C stretch backbone
*
9
939 cm −1
Structural proteins like collagen
*
32
C-C skeletal stretching in
protein
*
16
940 cm −1
Carotenoid
*
25
CH 2 rocking mode
*
44
941 cm −1
Skeletal modes (polysaccharides,
amylose)
*
7
Skeletal modes (polysaccharides,
amylopectin)
*
7
943 cm −1
Cyclic C-C, ring and C-NR2
stretch
*
14
Out-of-phase ring CH wag
*
14
945 cm −1
CH 6',5' out of plane
*
6
948 cm −1
Structural proteins like collagen
*
34
( Continued )
 
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