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
Proteins, amide I (α helix) in
normal tissues
*
46
Amide I, α-helix, ν(C= O) of
proteins collagen and elastin
*
17
1659 cm
−1
Amide I
*
77
Amide I vibration (collagen like
proteins)
*
50, 94
Amide C= O stretching
absorption for the α-folded
polypeptide films
*
102
Cholesterol band (associated to
atherosclerotic spectrum)
*
49
1660 cm
−1
Amide I band
*
*
22
Amide I
*
22
Amide I vibration mode of
structural proteins
*
49
ν(C= C)
cis
, lipids, fatty acids
*
*
7
C= C groups in unsaturated fatty
acids
*
2
Ceramide backbone
*
2
Amide I
*
60
Amide I, β-pleated sheet, and/or
random coil conformation
*
35
Proteins, amide I (α helix) in
cancerous tissues
*
46
1661 cm
−1
Amide I, α-helix
60
1662 cm
−1
Nucleic acid modes
*
45
Nucleic acid modes indicating the
nucleic acid content in tissues
*
68
Nucleic acid vibrational mode
*
4
1663 cm
−1
DNA
*
8
Proteins, including collagen I
*
8
1664/5 cm
−1
Amide I
*
3
C= O cytosine, uracyl
*
48
1665 cm
−1
Amide I (of collagen)
*
3
Amide I
*
3
Amide I (collagen assignment)
*
19
Amide I (disordered structure,
solvated)
*
*
7
ν
s
(C= O)
*
106
C= C stretch band (
cis
form)
*
58
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