Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Folding

Protein Folding

Protein Folding

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 Folding

Protein Folding

Cis-regulatory Sequences

Cis-regulatory Sequences

Cis-regulatory sequences are short fragments of non-coding DNA that are present on the same chromosomes as the genes that they regulate. These fragments serve as binding sites for transcriptional regulators, proteins that are responsible for controlling gene transcription and differential gene expression across cell types in eukaryotes. Cis-regulatory sequences can be close to the gene of interest or thousands of bases away in the DNA sequence; however, those sequences that are further away are...

Cis-regulatory Sequences

Cis-regulatory Sequences

Cis-regulatory sequences are short fragments of non-coding DNA that are present on the same chromosomes as the genes that they regulate. These fragments serve as binding sites for transcriptional regulators, proteins that are responsible for controlling gene transcription and differential gene expression across cell types in eukaryotes. Cis-regulatory sequences can be close to the gene of interest or thousands of bases away in the DNA sequence; however, those sequences that are further away are...

Protein Organization

Protein Organization

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Adrenodoxin alters human cytochrome P450 27A1 structure and reaction efficiency beyond supplying electrons.

Archives of biochemistry and biophysics·2025

Same author

Optimization of CYP27A1 recombinant protein expression.

Protein expression and purification·2025

Same author

Click catalysis and DNA conjugation using a nanoscale DNA/silver cluster pair.

Nanoscale·2024

Same author

Breaching the Fortress: Photochemistry of DNA-Caged Ag<sub>10</sub><sup>6</sup>.

The journal of physical chemistry. B·2023

Same author

Interrupted DNA and Slow Silver Cluster Luminescence.

The journal of physical chemistry. C, Nanomaterials and interfaces·2023

Same author

Mapping H<sup>+</sup> in the Nanoscale (A<sub>2</sub>C<sub>4</sub>)<sub>2</sub>-Ag<sub>8</sub> Fluorophore.

The journal of physical chemistry letters·2022

Search research articles

Related Experiment Video

Updated: Jun 6, 2026

Design and Synthesis of a Reconfigurable DNA Accordion Rack

Design and Synthesis of a Reconfigurable DNA Accordion Rack

Published on: August 15, 2018

Sequence length dictates repeated CAG folding in three-way junctions.

Natalya N Degtyareva¹, Courtney A Barber, Michael J Reddish

¹Department of Chemistry, Furman University, Greenville, SC 29613, USA.

|December 15, 2010

Summary

The number of CAG repeats in DNA influences its folding, impacting inherited neurological diseases. Longer repeats promote hairpin formation, crucial for disease progression.

More Related Videos

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Published on: December 3, 2015

Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules

Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules

Published on: April 12, 2019

Related Experiment Videos

Last Updated: Jun 6, 2026

Design and Synthesis of a Reconfigurable DNA Accordion Rack

Design and Synthesis of a Reconfigurable DNA Accordion Rack

Published on: August 15, 2018

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Published on: December 3, 2015

Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules

Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules

Published on: April 12, 2019

Area of Science:

Molecular Biology
Genetics
Biophysics

Background:

Inherited neurological diseases often stem from hairpin structures in repetitive DNA sequences.
DNA folding is dictated by base sequence and DNA context.

Purpose of the Study:

To investigate how the number of CAG repeats affects DNA intrastrand folding.
To understand the role of DNA secondary structure in the pathogenesis of neurological disorders.

Main Methods:

Utilized 2-aminopurine as a fluorescent probe to monitor DNA folding.
Compared the folding of (CAG)(8) and (CAG)(15) repeats in isolation and within a three-way junction context.

Main Results:

Intrastrand folding of CAG repeats is dependent on the number of repeats.
(CAG)(15) forms a stable hairpin structure, even when integrated into a duplex, unlike shorter (CAG)(8) repeats.
Longer CAG repeats overcome structural perturbations, reasserting their natural folding propensity.

Conclusions:

The secondary structure of CAG repeats is a critical factor in the length-dependent manifestation of inherited neurological diseases.
Cooperative interactions in longer repeat tracts stabilize hairpin formation, influencing disease progression.