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Related Concept Videos

Infrared (IR) Spectroscopy: Overview01:09

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...
IR Spectroscopy: Molecular Vibration Overview01:24

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...
Applications of IR Spectroscopy: Overview01:11

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 Spectrometers01:25

IR Spectrometers

There are two main infrared (IR) spectrophotometers: dispersive IR spectrometers and Fourier transform infrared (FTIR) spectrometers. In a dispersive IR spectrometer, a beam of infrared radiation produced by a hot wire is divided into two parallel equal-intensity beams using mirrors. One beam passes through the sample, while another is a reference beam. The beams then move through the monochromator, which separates the radiations into a continuous spectrum of different frequencies. The...
IR Spectrum01:19

IR Spectrum

When infrared (IR) radiation passes through a molecule, the bonds stretch or bend by absorbing the radiation. This absorption creates the molecule's absorption spectrum, which is the plot of its percentage transmittance versus wavenumber.
Transmittance is defined as the ratio of the radiant power passing through a sample to that from the radiation's source. Multiplying the transmittance by 100 gives the percent transmittance (%T), which varies between 100% (no absorption) and 0% (complete...
IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration01:16

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...

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Related Experiment Video

Updated: Jun 9, 2026

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

Published on: January 21, 2015

From structure to cellular mechanism with infrared microspectroscopy.

Lisa M Miller1, Paul Dumas

  • 1National Synchrotron Light Source, Brookhaven National Laboratory, Upton, NY, USA. lmiller@bnl.gov

Current Opinion in Structural Biology
|August 27, 2010
PubMed
Summary

Synchrotron Fourier Transform Infrared Microspectroscopy (FTIRM) uses infrared radiation and X-rays to link molecular structure with cellular function. This technique advances biological and biomedical research by providing insights into biochemical dynamics.

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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

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High-definition Fourier Transform Infrared (FT-IR) Spectroscopic Imaging of Human Tissue Sections towards Improving Pathology
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Atomic Force Microscopy Combined with Infrared Spectroscopy as a Tool to Probe Single Bacterium Chemistry
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Atomic Force Microscopy Combined with Infrared Spectroscopy as a Tool to Probe Single Bacterium Chemistry

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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

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Area of Science:

  • Structural biology
  • Biophysics
  • Spectroscopy

Background:

  • Integrating structural data with cellular function is a key goal in structural biology.
  • X-rays and infrared radiation are complementary electromagnetic probes.
  • Synchrotron radiation provides intense beams across a wide wavelength range.

Purpose of the Study:

  • To discuss the role of synchrotron Fourier Transform Infrared Microspectroscopy (FTIRM) in advancing functional biology.
  • To highlight recent achievements of synchrotron FTIRM.
  • To critically assess its contributions to biological and biomedical research.

Main Methods:

  • Utilizing synchrotron radiation for intense X-ray and far-infrared (THz) beams.
  • Employing X-ray crystallography for atomic structure determination.
  • Applying Fourier Transform Infrared Microspectroscopy (FTIRM) as a spectroscopic and imaging tool.

Main Results:

  • FTIRM is emerging as a powerful tool for correlating molecular structure with biochemical dynamics and function.
  • Synchrotron FTIRM bridges the gap between structural information and cellular context.
  • Recent achievements demonstrate its utility in biological and biomedical research.

Conclusions:

  • Synchrotron FTIRM is crucial for understanding molecular mechanisms in a cellular context.
  • The technique offers a unique approach to functional biology.
  • Its application significantly contributes to biological and biomedical advancements.