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Related Concept Videos

UV–Vis Spectrometers01:14

UV–Vis Spectrometers

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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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Ultraviolet and Visible (UV–Vis) Spectroscopy: Overview01:02

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Ultraviolet–visible (UV–visible or UV–Vis) spectroscopy is an analytical technique that investigates the interaction between matter and UV–Vis light within the electromagnetic spectrum. This method is widely used for its versatility, simplicity, and relatively quick data acquisition, making it valuable for both qualitative and quantitative analysis. When UV–Vis radiation passes through a material,  molecules absorb light depending on the energy required for...
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UV–Vis Spectrum01:30

UV–Vis Spectrum

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When light passes through a substance, a portion of the light is absorbed while the remaining light is reflected or transmitted. If the molecule absorbs light between the wavelengths of 180–400 nm range, the UV spectrum is obtained, and if it absorbs light in the 400–780 nm wavelength range, the visible spectrum is obtained.     
The UV–Vis spectrum of a molecule is the plot of its absorbance versus wavelength. The plot is drawn by taking molar...
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UV–Vis Spectroscopy: Beer–Lambert Law01:09

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The Beer-Lambert law describes the relationship between absorbance and concentration, which combines the principles established by scientists Johann Heinrich Lambert and August Beer. Lambert's law states that when light passes through a medium, the loss in intensity is directly proportional to the original intensity and the path length of the light. Beer's law proposed that the transmittance of a solution remains constant if the product of concentration and path length is constant. The modern...
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UV–Vis Spectroscopy: Molecular Electronic Transitions01:16

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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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UV–Vis Spectroscopy: Woodward–Fieser Rules01:29

UV–Vis Spectroscopy: Woodward–Fieser Rules

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UV–Visible absorption spectra of conjugated dienes arise from the lowest energy π → π* transitions. The light-absorbing part of the molecule is called the chromophore, and the substituents directly attached to the chromophore are called auxochromes. A strong correlation exists between the absorption maxima, λmax, and the structure of a conjugated π system. The Woodward–Fieser rules predict the value of λmax for a given structure by adding the...
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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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A method to probe protein structure from UV absorbance spectra.

Amadeo B Biter1, Jeroen Pollet1, Wen-Hsiang Chen1

  • 1National School of Tropical Medicine, Department of Pediatrics, Baylor College of Medicine, Houston, TX, 77030, USA; Texas Children's Hospital Center for Vaccine Development, Houston, TX, 77030, USA.

Analytical Biochemistry
|September 25, 2019
PubMed
Summary

A new method using UV absorbance ratios can determine protein foldedness. This technique offers a sensitive way to study protein stability, interactions, and refolding processes.

Keywords:
Protein conformationProtein denaturationProtein foldingProtein misfoldingProtein stabilityProtein structureProtein-protein interactionUV–Vis spectroscopy

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Area of Science:

  • Biochemistry
  • Spectroscopy
  • Protein Chemistry

Background:

  • Proteins absorb UV light due to aromatic amino acid residues: tryptophan (280 nm), tyrosine (275 nm), and phenylalanine (258 nm).
  • Quantifying protein structure and interactions often relies on biophysical techniques.

Purpose of the Study:

  • To introduce a novel, simple, and robust method for assessing protein foldedness using UV absorbance.
  • To demonstrate the utility of this method in probing various protein conformational states and interactions.

Main Methods:

  • Measuring UV absorbance of proteins at 280 nm, 275 nm, and 258 nm.
  • Calculating a ratio: [A280/A275 + A280/A258] to correlate with protein foldedness.

Main Results:

  • The calculated absorbance ratio serves as a sensitive indicator of protein foldedness.
  • This method effectively monitors protein unfolding and refolding.
  • The ratio is also applicable to studying disulfide bond formation, protein stability, and interactions.

Conclusions:

  • The [A280/A275 + A280/A258] ratio is a versatile and sensitive probe for protein foldedness.
  • This technique provides valuable insights into protein conformational changes and interactions without complex instrumentation.