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Infrared (IR) Spectroscopy: Overview

Infrared (IR) Spectroscopy: Overview

When electromagnetic radiation passes through a material, atoms or molecules transition from a lower to a higher energy state by absorbing radiation corresponding to the energy difference between the two states. The absorption of infrared (IR) radiation causes transitions between vibrational energy levels in a molecule. Therefore, IR spectroscopy is a useful analytical tool for determining the molecular structure of molecules.
Different compounds display unique properties due to their...

Applications of IR Spectroscopy: Overview

Applications of IR Spectroscopy: Overview

The non-destructive nature and ability to provide valuable chemical information make IR spectroscopy a versatile technique with broad applications in various scientific and industrial fields. IR spectroscopy is commonly used to identify and characterize organic and inorganic compounds. It provides information about the functional groups present in a molecule and the bonding between atoms. This helps in the structural elucidation of compounds during organic synthesis, pharmaceutical research,...

IR Spectroscopy: Molecular Vibration Overview

IR Spectroscopy: Molecular Vibration Overview

When Infrared (IR) radiation passes through a covalently bonded molecule, the bonds transition from lower to higher vibrational levels. The fundamental vibrational motions that result in infrared absorption can be classified as stretching or bending vibrations.
Stretching vibrations are vibrational motions that occur along the bond line, changing the bond length or distance between two bonded atoms. They are further distinguished as symmetric or asymmetric. In symmetric stretching, the...

IR and UV–Vis Spectroscopy of Carboxylic Acids

IR and UV–Vis Spectroscopy of Carboxylic Acids

In IR spectroscopy of carboxylic acids, the C=O bond shows a characteristic band between 1710 and 1760 cm⁻¹, and the O–H bond exhibits a broad band between 2500 and 3300 cm⁻¹.
However, the stretching absorptions for the C=O bond vary depending on the structure of carboxylic acids. The C=O bond of the free carboxylic acids shows a higher stretching frequency, 1760 cm−1, while H-bonded carboxylic acids (dimers) exhibit stretching absorptions at a lower frequency, 1710 cm−1. The C=O bond of the...

IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration

IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration

A covalently bonded heteronuclear diatomic molecule can be modeled as two vibrating masses connected by a spring. The vibrational frequency of the bond can be expressed using an equation derived from Hooke's law, which describes how the force applied to stretch or compress a spring is proportional to the displacement of the spring. In this case, the atoms behave like masses, and the bond acts like a spring.
According to Hooke's law, the vibrational frequency is directly proportional to the...

Raman Spectroscopy: Overview

Raman Spectroscopy: Overview

The underlying principle of Raman spectroscopy is based on the interaction between light and matter, specifically molecules' inelastic scattering of photons. When a monochromatic beam of light, typically from a laser source, interacts with a sample, most scattered light has the same frequency as the incident light. This is known as Rayleigh scattering.
However, a small fraction of the scattered light exhibits a frequency shift due to the exchange of energy between the incident photons and the...

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Related Experiment Video

Updated: May 8, 2026

High-definition Fourier Transform Infrared (FT-IR) Spectroscopic Imaging of Human Tissue Sections towards Improving Pathology

High-definition Fourier Transform Infrared (FT-IR) Spectroscopic Imaging of Human Tissue Sections towards Improving Pathology

Published on: January 21, 2015

Studying biomacromolecules with two-dimensional infrared spectroscopy.

Rachel E Hill¹, Neil T Hunt, Jonathan D Hirst

¹School of Chemistry, University of Nottingham, University Park, Nottingham, United Kingdom.

Advances in Protein Chemistry and Structural Biology

|September 11, 2013

Summary

Two-dimensional infrared (2DIR) spectroscopy offers enhanced structural insights into biomacromolecules by resolving complex vibrational spectra. This nonlinear technique tracks molecular dynamics on a subpicosecond timescale, revealing fundamental aspects of protein and nucleic acid structure.

Keywords:

Biomacromolecules Nucleic acids Proteins Two-dimensional Infrared Ultrafast

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Area of Science:

Nonlinear spectroscopy
Vibrational spectroscopy
Biophysical chemistry

Background:

Fourier transform infrared (FTIR) spectra of biomacromolecules are often congested.
Traditional vibrational spectroscopies provide limited structural detail.
Understanding biomacromolecular structure and dynamics is crucial.

Purpose of the Study:

To review recent studies utilizing 2DIR spectroscopy for biomacromolecules.
To showcase the potential of 2DIR spectroscopy in structural and dynamic analysis.
To highlight advancements in nonlinear spectroscopy for biological systems.

Main Methods:

Two-dimensional infrared (2DIR) spectroscopy, a nonlinear technique.
Utilizing subpicosecond timescales for time-domain molecular fluctuation analysis.
Application of well-developed theoretical and experimental techniques.

Main Results:

2DIR spectroscopy provides greater structural detail compared to traditional methods.
The technique allows for the study of molecular dynamics on a subpicosecond timescale.
Recent studies have provided insights into protein and nucleic acid structure and dynamics.

Conclusions:

2DIR spectroscopy is a powerful tool for investigating biomacromolecular structure and dynamics.
The method offers significant advantages over conventional vibrational spectroscopies.
Further research using 2DIR spectroscopy promises deeper understanding of biological molecules.