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UV–Vis Spectroscopy of Conjugated Systems01:32

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Organic compounds with conjugated double bonds show strong absorption features in the UV–visible region of the electromagnetic spectrum attributed to π → π* electronic excitations. Generally, a UV–vis absorption spectrum is recorded as a plot of absorbance vs wavelength. The wavelength of maximum absorbance, which manifests as a peak in the absorption spectrum, is denoted as λmax.
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In Ultraviolet–Visible (UV–Vis) spectroscopy, the absorption of electromagnetic radiation is used to probe the electronic structure of molecules. This technique provides insights into molecular electronic transitions, particularly the movement of electrons between different molecular orbitals. Radiation is absorbed if the energy of the electromagnetic radiation passing through the molecule is precisely equal to the energy difference between the excited and ground states. During this...
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Chirality at Nitrogen, Phosphorus, and Sulfur02:30

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Chirality is most prevalent in carbon-based tetrahedral compounds, but this important facet of molecular symmetry extends to sp3-hybridized nitrogen, phosphorus and sulfur centers, including trivalent molecules with lone pairs. Here, the lone pair behaves as a functional group in addition to the other three substituents to form an analogous tetrahedral center that can be chiral.
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IR Spectroscopy: Molecular Vibration Overview01:24

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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.
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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.
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The absorbance of UV and visible (UV–visible) radiations is measured using a UV–visible spectrophotometer. Deuterium lamps, which emit UV radiation, and tungsten lamps, which produce radiation in the visible region, are used as light sources in UV–visible spectrophotometers. A monochromator or prism is used for diffraction grating, i.e., to split the incoming radiation into different wavelengths. A system of slits is used to focus the desired wavelength on the sample cell.
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Updated: Apr 18, 2026

Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy
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Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy

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Proteins at interfaces probed by chiral vibrational sum frequency generation spectroscopy.

Elsa C Y Yan1, Zhuguang Wang, Li Fu

  • 1Department of Chemistry, Yale University , New Haven, CT 06511, United States.

The Journal of Physical Chemistry. B
|January 8, 2015
PubMed
Summary

Chiral vibrational sum frequency generation spectroscopy (SFG) offers a new way to study protein structures at interfaces. This label-free method provides real-time insights into protein secondary structures, orientations, and folding kinetics.

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Area of Science:

  • Biophysics
  • Spectroscopy
  • Materials Science

Background:

  • Protein structure characterization at interfaces is crucial for understanding biological processes and developing new biomaterials.
  • Existing methods face challenges in achieving in situ and real-time analysis of protein secondary structures at interfaces.
  • There is a need for advanced techniques that are selective for both interface and secondary structures.

Purpose of the Study:

  • To introduce and demonstrate the capabilities of chiral vibrational sum frequency generation spectroscopy (SFG) for analyzing protein structures at interfaces.
  • To showcase SFG's ability to provide vibrational optical signatures for distinguishing protein secondary structures.
  • To highlight SFG's application in probing protein orientations and folding kinetics in real-time.

Main Methods:

  • Utilizing chiral vibrational sum frequency generation spectroscopy (SFG), a vibrational spectroscopic technique.
  • Analyzing vibrational optical signatures, specifically the peptide N-H stretch and amide I modes.
  • Applying the method for in situ and real-time characterization of proteins at interfaces.

Main Results:

  • Chiral SFG successfully identified distinct vibrational optical signatures for various protein secondary structures.
  • The technique was applied to probe protein orientations and folding kinetics at interfaces.
  • SFG demonstrated its capability as a background-free, label-free, in situ, and real-time method.

Conclusions:

  • Chiral SFG is a powerful, versatile tool for studying protein secondary structures at interfaces.
  • The method offers label-free, real-time, and in situ analysis, overcoming limitations of previous techniques.
  • This advancement holds significant potential for research in proteins and other chiral biopolymers at interfaces.