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
1650 cm
−1
Amide I absorption
(predominantly the C= O
stretching vibration of the amide
C= O)
*
38, 52
(C= C) amide I
*
54
Protein amide I absorption
C= O, stretching C= C uracyl, NH
2
guanine
*
48
Peptide amide I
*
72, 100
Amide I
*
103
Carbonyl stretching
*
85
1650-60 cm
−1
C= C stretch band for the
nonconjugated
cis
configuration
*
58, 104,
105
1650-60 cm
−1
C-C stretch
*
58
1652 cm
−1
Amide I
*
69
1652/3 cm
−1
C
2
= O cytosine
*
48
Lipid (C= C stretch)
*
9
1653 cm
−1
Carbonyl stretch (C= O)
*
5
*
1
νC= O
1653/4 cm
−1
C= O, C= N, N-H of adenine,
thymine, guanine, cytosine
*
23
1654 cm
−1
Due to a combination of C= C
stretch and the amide I bands +
Amide I
*
24, 96
Amide I (collagen assignment)
C= C stretch
*
19
Amide I (C= O stretching mode of
proteins, α-helix conformation)/
C= C lipid stretch
*
*
19
9
Collagen
ν(C= C) of lipids
*
26
*
17
1655 cm
−1
Amide I (of collagen)
*
3
C= C (of lipids in normal tissues;
not that of amide I)
*
54
ν(C= O) amide I, α-helix, collagen
*
20, 33, 98
Amide I (C= O stretching mode of
proteins, α-helix conformation)/
C= C lipid stretch
*
9, 10
In normal tissues : C= C of lipids
(and not amide I)
*
20
C= O stretching of collagen and
elastin (protein assignment)
*
20
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