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Related Concept Videos

IR Spectrum Peak Splitting: Symmetric vs Asymmetric Vibrations01:08

IR Spectrum Peak Splitting: Symmetric vs Asymmetric Vibrations

Identical bonds within a polyatomic group can stretch symmetrically (in-phase) or asymmetrically (out-of-phase). Similar to hydrogen bonding, these vibrations also influence the shape of the IR peak. Generally, asymmetric stretching frequencies are higher than symmetric stretching frequencies. For example, primary amines exhibit two distinct IR peaks between 3300–3500 cm−1 corresponding to the symmetric and asymmetric N-H stretching, while secondary amines exhibit a single stretching vibration...
IR Frequency Region: X–H Stretching01:24

IR Frequency Region: X–H Stretching

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 the 3500–3100 cm−1 range. Even though both O−H and N−H bonds vibrate at a similar...

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Updated: Jun 29, 2026

Simulation, Fabrication and Characterization of THz Metamaterial Absorbers
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THz Anisotropy Identification using Tunable Compact Narrow Band THz Sources.

D K George1, A G Markelz1, Ian Mcnee2

  • 1Department of Physics, University at Buffalo, Buffalo NY USA.

International Conference on Infrared, Millimeter, and Terahertz Waves : [Proceedings]. International Conference on Infrared, Millimeter, and Terahertz Waves
|April 19, 2021
PubMed
Summary
This summary is machine-generated.

We used new compact terahertz (THz) sources to determine the anisotropy signature of protein crystals. This breakthrough offers turn-key spectroscopic systems for biomolecular research.

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Area of Science:

  • Biophysics
  • Spectroscopy
  • Crystallography

Background:

  • Terahertz (THz) spectroscopy is a valuable tool for analyzing biomolecular structures.
  • Characterizing anisotropy in protein crystals is crucial for understanding their properties.
  • Existing THz systems can be complex and lack tunability.

Purpose of the Study:

  • To demonstrate THz anisotropy signature determination in protein crystals.
  • To introduce novel, compact, tunable, narrow-band THz sources.
  • To enable turn-key spectroscopic systems for the biomolecular community.

Main Methods:

  • Utilized newly developed compact tunable narrow-band THz sources.
  • Applied THz spectroscopy to a protein crystal model.
  • Measured and analyzed the anisotropy signature.

Main Results:

  • Successfully determined the THz anisotropy signature of the protein crystal model.
  • Demonstrated the capability of the new THz sources for this application.
  • Validated the potential for turn-key spectroscopic systems.

Conclusions:

  • Compact, tunable THz sources facilitate efficient anisotropy determination in protein crystals.
  • The developed technology supports the creation of user-friendly spectroscopic systems for biomolecular studies.
  • This advancement aids in the structural and functional characterization of biomolecules.