FTIR and Raman Characteristic Peak Frequencies in Biological Studies - Vibrational Spectroscopy for Tissue Analysis - page 273

Table 8.1 ( Continued )
Major Characteristic Peak Frequencies Reported in the Literature

Reference
Number Peak Assignment FT-IR Raman

Amide C= O stretching
absorption for the β-form
polypeptide films

* 102

1630-80 cm −1 Due to the carbonyl stretching of

an amide group

* 30

1630-700 cm −1 Amide I region * 38

1632 cm −1 Ring C-C stretch of phenyl (2) * 6

1632/4 cm −1 C= C uracyl, C= O * 48

1634 cm −1 Amide I * 24

1635 cm −1 Differences in collagen content * 24

β-sheet structure of amide I * 83

1637 cm −1 Amide I band * 15

C= C uracyl, C= O * 48

Amide I band (both α-helix and
β-structure)

* 43

1638 cm −1 Intermolecular bending mode of

water

* 9

Very weak and broad ν 2 mode of
water

* 43

1638/9 cm −1 C= C thymine, adenine, N-H

guanine

* 48

1639 cm −1 Amide I * 77

1640 cm −1 Amide I band of protein and

H-O-H deformation of water

* 101

1640-80 cm −1 Amide I band (protein band) * 30, 95

1640-740 cm −1 C= O stretching modes * 1

1642 cm −1 C 5 methylated cytosine? * 48

1643 cm −1 Amide I band (arises from C= O

stretching vibrations)

* 62

1644 cm −1 Amide I * 77

1645 cm −1 Amide I (α-helix) * 9

1646 cm −1 Amide I * 74

C 5 methylated cytosine? * 48

C= O, stretching C= C uracyl, NH 2
guanine

* 48

1647 cm −1 Random coils * 43

1647/8 cm −1 Amide I in normal tissues;

in lower frequencies in cancer

* 74

1649 cm −1 Unordered random coils and

turns of amide I

* 83

C= O, C= N, N-H of adenine,
thymine, guanine, cytosine

* 23

( Continued )