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Related Concept Videos

X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are  scattered by the electron clouds around the sample atoms. The  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal crystal...

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Related Experiment Video

Updated: Jul 5, 2026

CD Spectroscopy to Study DNA-Protein Interactions
06:48

CD Spectroscopy to Study DNA-Protein Interactions

Published on: February 10, 2022

Circular dichroism to study protein interactions.

Sharon M Kelly1, Nicholas C Price1

  • 1University of Glasgow, Glasgow, United Kingdom.

Current Protocols in Protein Science
|April 23, 2008
PubMed
Summary
This summary is machine-generated.

Circular dichroism (CD) spectroscopy reveals protein structures and conformational changes upon ligand binding. This method quantizes interaction strength and the extent of structural alterations for reliable data.

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Last Updated: Jul 5, 2026

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Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Spectroscopy

Background:

  • Circular dichroism (CD) is a key spectroscopic technique.
  • It is utilized for analyzing protein structures in solution.
  • CD also monitors structural modifications during ligand interactions.

Purpose of the Study:

  • To detail the information obtainable from circular dichroism studies.
  • To outline experimental procedures for acquiring reliable CD data.
  • To explain how CD signals reflect protein-ligand interactions and conformational changes.

Main Methods:

  • Circular dichroism spectroscopy.
  • Analysis of spectral changes upon protein-ligand complex formation.
  • Methodological guidelines for experimental design and data acquisition.

Main Results:

  • CD signal changes correlate with protein-ligand complex formation.
  • Quantification of interaction strength is possible via CD.
  • Information on the nature and extent of conformational changes is derived.

Conclusions:

  • Circular dichroism is a valuable tool for studying protein structure and dynamics.
  • CD provides insights into the thermodynamics and structural basis of molecular recognition.
  • Adherence to proper experimental protocols ensures the generation of high-quality, reliable data.