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
838 cm −1
Deformative vibrations of amine
groups
*
28
840 cm −1
α-anomers
*
2
Glucose-saccharide band
(overlaps with acyl band)
*
2
Saccharide (α)
*
2
840-60 cm −1
Polysaccharide structure
*
29, 30
842 cm −1
Glucose
*
9
847 cm −1
Monosaccharides (α-glucose),
(C-O-C) skeletal mode
*
7
Disaccharide (maltose), (C-O-C)
skeletal mode
*
7
850 cm −1
Most probably due to single bond
stretching vibrations for the
amino acids and valine and
polysaccharides
*
29
Tyrosine (Fermi resonance of ring
fundamental and overtone)
*
7
850-950 cm −1
Signal free area of amphetamine
*
31
850-990 cm −1
Ring stretch, C-N-R2 stretch and
cyclic C-C-C bend
*
14
852 cm −1
Proline, hydroxyproline, tyrosine
*
3
Tyrosine ring breathing
*
12
Glycogen
*
8
Ring breathing of tyrosine and
ν(C-C) hydroxyproline ring
specific to collagen
*
17
853 cm −1
Ring breathing mode of tyrosine
and C-C stretch of proline ring
*
9, 10
Glycogen
*
8
853/4 cm −1
Structural proteins like collagen
*
32
854 cm −1
CH 2, 6 out-of-plane bending
*
*
6
(C-O-C) skeletal mode of
α-anomers (polysaccharides,
pectin)
*
7
Protein peak
*
17
Ring breathing of tyrosine and
ν(C-C) hydroxyproline ring
specific to collagen
*
17
Ring breathing in tyrosine/C-C
stretching in proline
*
16
855 cm −1
Proline, tyrosine
*
20
( Continued )
 
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