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
ν
as
(COO
−
) (polysaccharides,
pectin)
*
7
1606 cm
−1
Adenine vibration in DNA
*
23
1607 cm
−1
Tyrosine, phenylalanine ring
vibration
*
43
1608/9 cm
−1
Cytosine (NH
2
)
*
21
1609 cm
−1
Adenine vibration in DNA
*
23
Haemoglobin
*
60
1610 cm
−1
Cytosine (NH
2
)
*
21
C= C bending in phenylalanine
and tyrosine
*
16
1613 cm
−1
Ring stretch with CO conjugation
*
14
1614 cm
−1
Tyrosine
*
3
1615 cm
−1
Tyrosine, Tryptophan, C= C
(protein)
*
12
1616 cm
−1
C= C stretching mode of tyrosine
and tryptophan
*
9, 10
1617 cm
−1
ν(C
a
C
b
), observed in the spectra
of single human RBC
*
22
1618 cm
−1
ν(C= C), tryptophan (protein
assignment)
*
20
ν(C= C), porphyrin
*
20
Tryptophan
*
20
Bound and free NADH
*
54
Ring C-C stretch of phenyl(2)
*
6
1620 cm
−1
Peak of nucleic acids due to the
base carbonyl stretching and
ring breathing mode
*
50
ν(C= C), porphyrin
*
33
Haemoglobin
*
60
1620-40 cm
−1
Bending vibration of R-CONHR
group
*
30
1620-750 cm
−1
In-plane double end vibrations of
bases. The spectra in this region
are very sensitive to base-
pairing interactions and
base-stacking effects, i.e., effects
of hydrogen bond formation.
*
24, 30
1622 cm
−1
Tryptophan
*
3
Tryptophan and/or β-sheet
*
3
Tryptophan (IgG?)
*
43
1628 cm
−1
C
α
= C
α
stretch
*
6
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