INFRARED SPECTROSCOPY

• Much higher wavelength

• "Infra red" covers the range of the electromagnetic spectrum
between 0.78 and 1000 µm.
Infra Red Absorption Spectra
Theory of infra red absorption
• IR radiation does not have enough energy to induce
electronic transitions as seen with UV.
• Absorption of IR is restricted to compounds with
small energy differences in the possible vibrational
and rotational states.
• For a molecule to absorb IR, the vibrations or
rotations within a molecule must cause a net change
in the dipole moment of the molecule.
Infrared Spectroscopy
• The fundamental frequencies observed are characteristic of the functional
groups concerned, hence the term fingerprint .
• As the number of functional groups increases in more complex molecules,
the absorption bands become more difficult to assign.
• However, groups of certain bands regularly appear near the same
wavelength and may be assigned to specific functional groups.
• Such group frequencies are thus extremely helpful in structural diagnosis.
• A more detailed analysis of the structure of a molecule is possible, because
the wavenumber associated with a particular functional group varies
slightly, owing to the influence of the molecular environment.
• For example, it is possible to distinguish between C–H vibrations in
methylene (–CH2 –) and methyl groups (–CH3 ).
• Mid-infrared is energetic enough to excite molecular
vibrations to higher energy levels.
• The wavelength of infrared absorption bands is characteristic
of specific types of chemical bonds, and infrared spectroscopy
finds its greatest utility for identification of organic and
organometallic molecules.
• If the frequency of the radiation matches the vibrational
frequency of the molecule then radiation will be absorbed,
causing a change in the amplitude of molecular vibration.
Organic structure determination
How do we know:

• How atoms are connected together?

• Which bonds are single, double, or triple?
• What functional groups exist in the molecule?
• If we have a specific stereoisomer?

The field of organic structure determination

attempts to answer these questions.
Infrared Spectroscopy (IR) –
• Triggering molecular vibrations through irradiation with
infrared light.
• Provides mostly information about the presence or absence
of certain functional groups.
SPECTROSCOPY - Study of spectral information

Physical response Detecting

Molecule
stimulus instrument

Visual (most common)

representation, or
Spectrum

Upon irradiation with infrared light, certain bonds respond

by vibrating faster. This response can be detected and
translated into a visual representation called a spectrum.
• Infrared radiation is largely thermal energy.
• It induces stronger molecular vibrations in covalent bonds, which
can be viewed as springs holding together two masses, or atoms.

Specific bonds respond to (absorb) specific frequencies

Possible stretching vibrations

in acetaldehyde
Vibrational modes

The most useful bands in an infrared spectrum correspond to stretching

frequencies (Types of Vibrational modes)
Vibrational modes
Infrared spectra: Wave number
UV-visible spectra: Wavelength

Wave number

Vibrational Frequencies

Where, v = Frequency,
k = Force constant
m1 and m2 are the masses of the two atoms
Approximate frequency of the C-H stretching vibration
k = 5.0 X 105 g S-2
mass of carbon atom = 20 x 10-24 g
mass of hydrogen atom = 1.6 x 10-24 g

Vibrational Frequencies
Wave number =
Speed of light

It is 3100 cm-1 for C-H stretching vibration

• Frequency on the basis of the bond strength (C-C/ C=C)

• Frequency on the basis of mass (C-C/ C-H)

C-H , N-H , O-H , and F-H

Regions of wavelength range

Region Wavelength Wavenumber Frequency

Range, um Range,cm-1 Range, Hz
Near 0.78-2.5 12800-4000 3.8x1014-1.2x1014

Middle 2.5-50 4000-200 1.2x1014-6.0x1012

Far 50-1000 200-10 6.0x1012-3.0x1011

Most used 2.5-15 4000-610 1.2x1014-2.0x1013

TRANSMISSION vs. ABSORPTION

Transmitted light
IR Chemical
Detector
source sample

From all the frequencies it receives, the chemical

sample can absorb (retain) specific frequencies and
allow the rest to pass through it (transmitted light).
AN IR SPECTRUM
Transmitted (or absorbed) frequencies
vs.
Intensity of the transmission (or absorption)

Spectrum in absorption mode. Spectrum in transmission mode

CLASSIFICATION OF IR BANDS
INFRARED ACTIVE BONDS
Only polar bonds display bands in the IR spectrum.

The intensity of the bands depends on the magnitude of the

dipole moment
Information obtained from IR spectra

•Presence or absence of specific functional groups.

•IR can provide a molecular fingerprint.

•IR does not provide detailed information of molecular formula

or structure.

•It has very limited in scope

IR absorption range
The typical IR absorption range for covalent bonds is 600 - 4000 cm-1. The
graph shows the regions of the spectrum where the following types of bonds
normally absorb. For example a sharp band around 2200-2400 cm-1 would
indicate the possible presence of a C-N or a C-C triple bond.
The fingerprint region
Although the entire IR spectrum can be used as a fingerprint for the purposes of
comparing molecules, the 600 - 1400 cm-1 range is called the fingerprint region.
This is normally a complex area showing many bands, frequently overlapping each
other. This complexity limits its use to that of a fingerprint, and should be ignored
by beginners when analyzing the spectrum.

Focus your analysis on this region. This is where most stretching Fingerprint region: complex and difficult to
frequencies appear. interpret reliably.
Applications
Identification of synthesized compounds, or identification of
sample constituents (e.g. in food) when coupled to a separating method
such as gas chromatography (GC–IR).

e.g. Substance which has the elemental formula C14H280

Rate of reactions
• Groups are consumed or generated in the enzymatic reaction
• The loss or appearance of or even shifting of bands
Study of conformation
• IR is increasingly used for analysis of peptides and proteins. The
peptide bond gives rise to nine characteristic bands, named amide A,
B, I, II, III, . . ., VII. The amide I (1600–1700 cm-1) and amide II
(1500–1600 cm-1) bands are the major contributors to the protein
infrared spectrum.
Interaction between molecules

• Interchain hydrogen bonds

- Hydrogen bond between an N~H and a C=O