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
1203 cm
−1
C-C
6
H
5
stretch mode (one of C-C
ring vibration to be expected in
aromatic structure of xylene)
*
15
1204 cm
−1
Amide III and CH
2
wagging
vibrations from glycine
backbone and proline side
chains
*
24
Vibrational modes of collagen
proteins; amide III
*
83
C-O-C, C-O dominated by the
ring vibrations of
polysaccharides C-O-P, P-O-P
*
77, 86
Collagen
*
*
40, 69
Tyrosine, phenylalanine (IgG?)
*
43
Ring stretch, in-plane CH bend,
CH
2
twist
14
1205 cm
−1
Differences in collagen content
*
24
C-O-C, C-O dominated by the
ring vibrations of
polysaccharides C-O-P, P-O-P
*
66, 77
1206 cm
−1
Amide III
*
50
Collagen
*
51
Hydroxyproline, tyrosine
(collagen assignment)
*
19
Hydroxyproline, tyrosine
*
9
1207 cm
−1
PO
2
−
asymmetric (phosphate I)
*
50
1208 cm
−1
ν(C-C
6
H
5
), tryptophan,
phenylalanine (protein
assignment)
*
20, 33
Tryptophan
*
3
A, T (ring breathing modes of the
DNA/RNA bases); amide III
(protein)
*
12
1209 cm
−1
PO
2
−
asymmetric (phosphate I)
*
48
Tryptophan and phenylalanine
ν(C-C
6
H
5
) mode
*
9, 10
1210 cm
−1
C-C
6
H
5
stretching mode in
tyrosine and phenylalanine
*
87
ν
18
(δ: C
m
H), observed in the
spectra of single human RBC
*
22
Haemoglobin
*
60
Tryptophan
*
*
35
1212 cm
−1
PO
2
−
asymmetric (phosphate I)
*
48
(
Continued
)
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