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Related Concept Videos

Infrared (IR) Spectroscopy: Overview01:09

Infrared (IR) Spectroscopy: Overview

3.7K
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...
3.7K
IR Spectroscopy: Molecular Vibration Overview01:24

IR Spectroscopy: Molecular Vibration Overview

3.6K
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...
3.6K
IR Frequency Region: Fingerprint Region01:03

IR Frequency Region: Fingerprint Region

1.5K
IR spectra are divided into two main regions: the diagnostic region and the fingerprint region. The diagnostic region of the spectrum lies above 1500 cm−1. The absorptions resulting from single-bond vibrations of the N–H, C–H, and O–H stretch at higher wavenumbers and appear on the left side of the spectrum. The stretching absorptions of the C≡C and C≡N occur between 2100–2300 cm−1. In contrast, those arising from stretching absorptions of the...
1.5K
IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration01:16

IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration

2.2K
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...
2.2K
IR Spectrum01:19

IR Spectrum

1.6K
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%...
1.6K
IR Frequency Region: X–H Stretching01:24

IR Frequency Region: X–H Stretching

1.2K
In IR spectroscopy, signals produced by the X−H bonds (such as C−H, O−H, or N−H) can be observed in the frequency range of  2700–4000 cm–1. The C−H stretching vibration forms sharp bands in the region 2850–3000 cm–1. The presence of the O−H stretching vibration leads to the forming of an absorption band in the frequency range 3650–3200 cm−1. At the same time, N−H stretching can be confirmed by absorption bands in...
1.2K

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In situ FTIR Spectroscopy as a Tool for Investigation of Gas/Solid Interaction: Water-Enhanced CO2 Adsorption in UiO-66 Metal-Organic Framework
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Infrared spectroscopy probes ion binding geometries.

Sean C Edington1, Stephanie Liu2, Carlos R Baiz2

  • 1Department of Chemistry, Yale University, New Haven, CT, United States.

Methods in Enzymology
|April 23, 2021
PubMed
Summary

Infrared (IR) spectroscopy is a powerful tool for studying enzyme ion binding sites. This chapter details how to use IR spectroscopy for enzymology, focusing on ion binding and providing practical guidance with examples.

Keywords:
FTIRInfrared spectroscopyIon bindingProtein binding siteProtein structure

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Area of Science:

  • Biophysical Chemistry
  • Enzymology
  • Spectroscopy

Background:

  • Infrared (IR) spectroscopy offers high structural sensitivity and is applicable to aqueous samples, making it ideal for enzymology.
  • Its utility is further enhanced by time-resolved techniques, protein labeling, and other advanced methods.
  • Understanding ion binding sites in enzymes is crucial for elucidating their mechanisms.

Purpose of the Study:

  • To provide the fundamental physical background and literature context for using IR spectroscopy in enzymology.
  • To focus on the specific application of IR spectroscopy for interrogating ion binding sites.
  • To offer practical guidance on sample preparation, data collection, and spectral interpretation.

Main Methods:

  • Utilizing Infrared (IR) spectroscopy for molecular structure and behavior analysis.
  • Applying specialized experimental schemes, including ultrafast time resolution and protein labeling.
  • Employing lanthanide ions binding to calmodulin as a model system for ion binding studies.

Main Results:

  • Demonstrated the versatility and power of IR spectroscopy in enzymological studies.
  • Highlighted the effectiveness of IR spectroscopy in probing ion binding sites.
  • Provided a practical framework for researchers to collect and analyze IR spectroscopic data.

Conclusions:

  • IR spectroscopy is a valuable and versatile technique for enzymology, particularly for studying ion binding.
  • Advanced IR spectroscopy methods significantly extend its capabilities.
  • This chapter equips readers with the knowledge to apply IR spectroscopy in their own ion binding research.