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
Amide I (of proteins in α-helix
conformation)
*
56, 65
Amide I (νC= O, δC-N, δN-H)
*
48
C= O cytosine
*
23
C= O, C= N, N-H of adenine,
thymine, guanine, cytosine
*
48
Peak of nucleic acids due to the
base carbonyl stretching and
ring breathing mode
*
50
Amide I has some overlapping
with the carbonyl stretching
modes of nucleic acid
*
51
Amide I of proteins
*
33, 35, 41
Amide I (collagen assignment)
*
19
Amide I (typically associated
with collagen)
*
91
Amide I (α-helix)
*
7
Protein amide I band (C= O
stretching mode of proteins,
indicating mainly α-helix
conformation)
*
35
C= O stretching of collagen and
elastin
*
35
1655-80 cm
−1
T, G, C (ring breathing modes of
the DNA/RNA bases); amide I
(protein)
*
12
1656 cm
−1
Amide I
*
19, 76
C
2
= O cytosine
*
48
ν(C= C)
cis
(phospholipids)
*
43
C= C (lipids)
*
43
Amide I (proteins)
*
43
Amide I, α-helix, ν(C= O) of
proteins collagen and elastin
*
17
1657 cm
−1
Fatty acids
*
24, 25
α-helical structure of amide I
*
83
Amide I (collagen assignment)
*
19
Triglycerides (fatty acids)
*
49
1658 cm
−1
C= O, stretching C= C uracyl, NH
2
guanine
*
49
Amide I
*
50
Amide I (α-helix)
*
43
*
1
(
Continued
)
νC= O
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