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Related Concept Videos

Infrared (IR) Spectroscopy: Overview01:09

Infrared (IR) Spectroscopy: Overview

6.3K
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...
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IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration01:16

IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration

3.4K
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...
3.4K
IR Spectroscopy: Molecular Vibration Overview01:24

IR Spectroscopy: Molecular Vibration Overview

5.6K
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...
5.6K
IR Frequency Region: Fingerprint Region01:03

IR Frequency Region: Fingerprint Region

2.1K
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...
2.1K
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

1.7K
The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse....
1.7K
Applications of IR Spectroscopy: Overview01:11

Applications of IR Spectroscopy: Overview

2.7K
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,...
2.7K

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Related Experiment Video

Updated: Mar 9, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.

Ayanjeet Ghosh1, Joshua S Ostrander1, Martin T Zanni1

  • 1Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.

Chemical Reviews
|January 7, 2017
PubMed
Summary
This summary is machine-generated.

Two-dimensional infrared (2D IR) spectroscopy is a powerful technique for studying protein dynamics across various timescales. This method provides unique structural and dynamical insights crucial for understanding protein function in biophysics and biomedical sciences.

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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:

  • Protein biophysics
  • Spectroscopy
  • Structural biology

Background:

  • Proteins exhibit structural fluctuations across a wide range of timescales, from picoseconds to minutes.
  • Understanding these dynamics is essential for elucidating protein function.
  • Traditional structural biology techniques may not fully capture these dynamic processes.

Purpose of the Study:

  • To review the principles of two-dimensional infrared (2D IR) spectroscopy.
  • To demonstrate the impact of 2D IR on protein biophysics.
  • To highlight its utility in obtaining otherwise inaccessible structural and dynamical data.

Main Methods:

  • Review of two-dimensional infrared (2D IR) spectroscopy principles.
  • Analysis of experimental applications of 2D IR in protein studies.
  • Discussion of technological advancements in 2D IR.

Main Results:

  • 2D IR spectroscopy uniquely probes protein structures and dynamics across multiple timescales.
  • It provides structural and dynamical data difficult to obtain with standard methods.
  • Technological developments are expanding its applicability in biomedical sciences.

Conclusions:

  • 2D IR spectroscopy is a versatile tool for characterizing protein structure and dynamics.
  • Its application has significantly advanced the field of protein biophysics.
  • Ongoing developments promise broader impact in biomedical research.