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
871 cm
−1
CH
2,2'
out-of-plane bending
*
6
873 cm
−1
Hydroxyproline, tryptophan
*
3
874 cm
−1
CH
2,2'
out-of-plane bending
*
6
C-C stretching, hypro (collagen
assignment)
*
19
875 cm
−1
Antisymmetric stretch vibration
of choline group
N
+
(CH
3
)
3
, characteristic for
phospholipids
*
2
Phosphatidylcholine,
sphingomyelin
*
2
Hydroxyproline (of collagen)
*
35
876 cm
−1
ν(C-C), hydroxyproline (protein
assignment)
*
20
C-C stretching, hydroxyproline
(collagen assignment)
*
19
*
17
ν(C-C), hydroxyproline in tumours
878 cm
−1
C
3'
endo/anti
(A-form helix)
conformation
*
23
879 cm
−1
Hydroxyproline, tryptophan
*
3
880 cm
−1
Tryptophan, δ(ring)
*
7
883 cm
−1
ρ(CH
2
) (protein assignment)
*
33
884 cm
−1
Proteins, including collagen I
*
8
885 cm
−1
Disaccharide (cellobiose),
(C-O-C) skeletal mode
*
7
886 cm
−1
Ring deformation and symmetric
C-N-C stretch
*
14
889 cm
−1
C-C, C-O deoxyribose
*
36
890 cm
−1
Protein bands
*
24, 25
C
3
'
endo/anti
(A-form helix)
conformation
*
23
C
2
'
endo/anti
(B-form helix)
conformation
*
23
Structural protein modes of
tumours
*
26
β-anomers
*
2
Ring deformation and symmetric
C-N-C stretch
*
14
891 cm
−1
Saccharide band (overlaps with
acyl band)
*
2
892 cm
−1
C-C, C-O deoxyribose
*
23
Fatty acid, saccharide (β)
(
Continued
)
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