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$X-ray Diffraction of Biological Samples$ 01:10

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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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

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The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.

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Related Experiment Video

Updated: Jul 4, 2026

CD Spectroscopy to Study DNA-Protein Interactions

CD Spectroscopy to Study DNA-Protein Interactions

Published on: February 10, 2022

Analysis of PrP conformation using circular dichroism.

Sen Han¹, Andrew F Hill

¹Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Australia.

Methods in Molecular Biology (Clifton, N.J.)

|June 26, 2008

Summary

Recombinant prion proteins (recPrP) are crucial models for studying prion diseases. Circular dichroism is a key method for analyzing structural changes in prion protein conversion, essential for understanding disease pathogenesis.

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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Published on: December 12, 2017

Area of Science:

Neuroscience
Biochemistry
Structural Biology

Background:

Prion diseases are linked to the conversion of cellular prion protein (PrP(C)) to its pathogenic form (PrP(Sc)).
This conversion involves a significant increase in beta-sheet content, altering protein structure and function.
Recombinant prion proteins (recPrP) serve as valuable models for investigating these processes.

Purpose of the Study:

To discuss the principles of circular dichroism (CD) spectroscopy.
To highlight the applications of CD in prion disease research.
To explain how CD monitors structural changes during prion protein conversion.

Main Methods:

Circular dichroism (CD) spectroscopy is detailed as a primary technique.
The chapter focuses on CD's role in analyzing structural alterations in prion protein mutants and oligomers.
CD is presented as a popular method for monitoring conformational changes.

Main Results:

CD spectroscopy effectively detects changes in secondary structure, particularly beta-sheet content.
The method aids in characterizing the structural landscape of recombinant prion proteins.
CD provides insights into the structural basis of PrP(Sc) formation.

Conclusions:

Circular dichroism is an indispensable tool in prion disease research.
Understanding structural changes via CD is vital for elucidating prion pathogenesis.
CD facilitates the study of PrP(C) to PrP(Sc) conversion and its implications.