Related Experiment Video
Updated: Feb 18, 2026

11:27
Studying DNA Looping by Single-Molecule FRET
Published on: June 28, 2014
15.9K
Kinetically Trapped Ligand Binding in DNA Tandem Repeats.
Rabia Tahir1, Shankar Pandey1, Jacob Haller1
1Department of Chemistry and Biochemistry, Kent State University, Kent, Ohio 44240, United States.
Biochemistry
|February 17, 2026
Summary
Ligand binding to DNA tandem repeats can lead to kinetically trapped states, not just stable ones. This groundbreaking finding reveals a new mechanism in molecular interactions within the genome.
Area of Science:
- Genomics
- Molecular Biology
- Biophysics
Background:
- Tandem DNA repeats are prevalent in the human genome, influencing gene regulation.
- Investigating ligand binding to these repeats is difficult with traditional methods like NMR and X-ray crystallography due to ensemble averaging.
Purpose of the Study:
- To investigate the binding mechanism between netropsin and adenine-thymine (A-T) DNA repeats using single-molecule techniques.
- To explore the potential for kinetically trapped states in ligand-DNA interactions within tandem repeats.
Main Methods:
- Utilized optical tweezers, a single-molecule technique with high sensitivity and temporal resolution.
- Interrogated the binding of netropsin, a DNA minor groove binder, to individual recognition sites in A-T DNA repeats.
Main Results:
- Discovered that netropsin binding to A-T DNA repeats favors kinetically trapped states over thermodynamically stable ones.
- Provided the first direct demonstration of kinetically trapped misbinding between a ligand and DNA tandem repeats.
Conclusions:
- Ligand binding to DNA tandem repeats can result in kinetically trapped states, a novel finding in molecular interactions.
- This mechanism may be fundamental to ligand-receptor interactions in biological systems and influence biological activities.
More Related Videos
Related Concept Videos
Cooperative Binding of Transcription Regulators
7.4K
Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome. Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
7.4K
Single-Strand DNA Binding Proteins
16.8K
For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
16.8K
Conserved Binding Sites
5.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.2K
Ligand Binding and Linkage
5.7K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.7K
DNA Topoisomerases
36.1K
Topoisomerases are enzymes that relax overwound DNA molecules during various cell processes, including DNA replication and transcription. These enzymes regulate positive and negative DNA supercoiling without changing the nucleotide sequence. DNA overwinding in a clockwise direction results in positively supercoiled DNA, whereas underwinding in a counterclockwise direction produces negatively supercoiled DNA.
Types and Mechanism of action
Topoisomerases are divided into two main types. ...
Types and Mechanism of action
Topoisomerases are divided into two main types. ...
36.1K
Translesion DNA Polymerases
11.3K
Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
11.3K

