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
1263 cm
−1
T, A (ring breathing modes of the
DNA/RNA bases); = C-H bend
(protein)
*
12
1264 cm
−1
Triglycerides (fatty acids)
*
49
Ring stretch
*
14
δ(= CH) of lipids
*
17
1265 cm
−1
PO
2
−
asymmetric (phosphate I)
*
48
CH
α'
rocking
*
6
Amide III of collagen
*
41
Amide III (collagen assignment)
*
19
Amide III
*
33, 35
ν(CN),δ(NH) amide III, α-helix,
collagen (protein assignment)
*
33
Phenylalanine stretching
(C-C6H5) mode
*
35
1266 cm
−1
Amide III (of proteins in the
α-helix conformation)
*
3, 20
ν(CN), δ(NH) amide III, α-helix,
collagen, tryptophan (protein
assignment)
*
20
δ (= C-H)
cis
*
7
Amide III (α-helix)
*
43
1267 cm
−1
C-H (lipid in normal tissue)
*
54
Amide III (collagen assignment)
1268 cm
−1
δ (= C-H) (phospholipids)
*
43
Ring stretch
*
14
1268/9 cm
−1
Amide III (collagen assignment)
*
19
1269 cm
−1
Structural proteins like collagen
*
32
Cytosine (ring breathing modes
of the DNA/RNA bases)
*
4
1270 cm
−1
Typical phospholipids
*
54
Amide III band in proteins
*
89, 90
Has traditionally been attributed
to Amide III, a C-N stretch from
alpha helix proteins
*
91
C= C groups in unsaturated fatty
acids
*
2
1272/3 cm
−1
CH
α'
rocking
*
*
6
1275 cm
−1
Amide III
*
7
1276 cm
−1
N-H thymine
*
48
(
Continued
)
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