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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

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: May 16, 2026

CD Spectroscopy to Study DNA-Protein Interactions
06:48

CD Spectroscopy to Study DNA-Protein Interactions

Published on: February 10, 2022

Circular dichroism in protein folding studies.

David T Clarke1

  • 1Central Laser Facility, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Didcot, Oxfordshire, United Kingdom.

Current Protocols in Protein Science
|November 16, 2012
PubMed
Summary

Protein folding studies are crucial for understanding diseases caused by protein misfolding. Ultraviolet circular dichroism (CD) monitors protein structure changes in solution, aiding in disease research.

Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology
  • Biophysical Chemistry

Background:

  • Protein folding is essential for biological function.
  • Misfolded proteins are linked to various human and animal diseases.
  • Studying protein folding dynamics requires high-time-resolution methods.

Purpose of the Study:

  • To describe methods for studying protein folding using ultraviolet circular dichroism (CD).
  • To provide practical guidance for performing CD experiments in protein folding research.
  • To identify and offer solutions for common challenges in CD spectroscopy of proteins.

Main Methods:

  • Utilizing ultraviolet circular dichroism (CD) spectroscopy.
  • Monitoring changes in protein secondary and tertiary structure in solution.

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

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Last Updated: May 16, 2026

CD Spectroscopy to Study DNA-Protein Interactions
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CD Spectroscopy to Study DNA-Protein Interactions

Published on: February 10, 2022

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

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  • Employing millisecond time-resolution measurements.

    • Main Results:

    • Detailed procedures for conducting CD experiments on protein folding are presented.
    • Commonly encountered issues during CD experiments are identified.
    • Practical solutions and troubleshooting tips for CD spectroscopy are provided.

    Conclusions:

    • Ultraviolet circular dichroism (CD) is a valuable technique for studying protein folding dynamics.
    • The described methods enable researchers to effectively monitor protein structural changes.
    • This unit serves as a practical guide for researchers investigating protein folding and misfolding-related diseases.