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
1597 cm −1
C= N, NH 2 adenine
*
48
1600 cm −1
Ring stretch with CO conjugation
*
14
1600-50 cm −1
C= C stretching vibrations from
the aromatic rings
*
1
1600-700 cm −1
Amide I
*
4
Amide I (due mostly to the C= O
stretching vibrations of the
peptide backbone)
*
30
1600-715 cm −1
In-plane double bond vibrations
of the nucleotide bases
*
47
1600-720 cm −1
The region of the amide I band of
tissue proteins (highly sensitive
to the conformational changes in
the secondary structure) (Amide
I band is due to in-plane
stretching of the C= O bond,
weakly coupled to stretching of
the C-N and in-plane bending
of the N-H bond.)
*
83
1600-800 cm −1
Amide I band of proteins; due to
C= O stretching
*
12, 89
Amide I (which is due mostly to
the C= O stretching vibrations of
the peptide backbone; has been
used the most for structural
studies due to its high sensitivity
to small changes in molecular
geometry and hydrogen
bonding of peptide group)
*
24
Amide I of proteins
*
35
1601/2 cm −1
C= N cytosine, N-H adenine
*
48
1602 cm −1
Phenylalanine
*
20
δ(C= C), phenylalanine (protein
assignment)
*
3
1603 cm −1
C= C in-plane bending mode of
phenylalanine and tyrosine
*
9, 10
Ring C-C stretch of phenyl (1)
*
6
1603/4 cm −1
C= N, NH 2 adenine
*
48
1604 cm −1
Adenine vibration in DNA
*
23
1605 cm −1
Cytosine (NH 2 )
*
21
Ring C-C stretch of phenyl (1)
*
6
Phenylalanine, tyrosine, C= C
(protein)
*
12
( Continued )
 
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