Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

6.7K
Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
6.7K
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

16.7K
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...
16.7K
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

18.1K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
18.1K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.8K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.8K
Protein and Protein Structure02:15

Protein and Protein Structure

88.2K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
88.2K
Protein Networks02:26

Protein Networks

4.6K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.6K

You might also read

Related Articles

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

Sort by
Same author

Advancing synthesis-free and enzyme-free rewritable DNA memory through frameshift encoding and nanopore duplex interruption decoding.

PNAS nexus·2025
Same author

Real-time label-free detection of dynamic aptamer-small molecule interactions using a nanopore nucleic acid conformational sensor.

Proceedings of the National Academy of Sciences of the United States of America·2023
Same author

Selective covalent capture of a DNA sequence corresponding to a cancer-driving C>G mutation in the <i>KRAS</i> gene by a chemically reactive probe: optimizing a cross-linking reaction with non-canonical duplex structures.

RSC advances·2022
Same author

Silver(I) ions modulate the stability of DNA duplexes containing cytosine, methylcytosine and hydroxymethylcytosine at different salt concentrations.

RSC advances·2019
Same author

Biomedical diagnosis perspective of epigenetic detections using alpha-hemolysin nanopore.

AIMS materials science·2019
Same author

Single Locked Nucleic Acid-enhanced nanopore genetic discrimination of pathogenic serotypes and cancer driver mutations.

Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual International Conference·2018

Related Experiment Video

Updated: Feb 9, 2026

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
05:37

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

1.3K

Encapsulating a single G-quadruplex aptamer in a protein nanocavity.

Ji Wook Shim1, Li-Qun Gu

  • 1Department of Biological Engineering and Dalton Cardiovascular Research Center University of Missouri, Columbia, Missouri 65211, USA.

The Journal of Physical Chemistry. B
|June 20, 2008
PubMed
Summary

This study uses the alpha-hemolysin (alphaHL) protein pore to trap and study thrombin-binding aptamer (TBA) G-quadruplexes. Changes in pore conductance reveal DNA unfolding and translocation dynamics.

More Related Videos

Aptamer-Based Target Detection Facilitated by a 3-Stage G-Quadruplex Isothermal Exponential Amplification Reaction
03:38

Aptamer-Based Target Detection Facilitated by a 3-Stage G-Quadruplex Isothermal Exponential Amplification Reaction

Published on: October 6, 2022

1.9K
Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
08:28

Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers

Published on: September 19, 2017

8.7K

Related Experiment Videos

Last Updated: Feb 9, 2026

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
05:37

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

1.3K
Aptamer-Based Target Detection Facilitated by a 3-Stage G-Quadruplex Isothermal Exponential Amplification Reaction
03:38

Aptamer-Based Target Detection Facilitated by a 3-Stage G-Quadruplex Isothermal Exponential Amplification Reaction

Published on: October 6, 2022

1.9K
Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers
08:28

Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers

Published on: September 19, 2017

8.7K

Area of Science:

  • Biotechnology
  • Nanotechnology
  • Molecular Biology

Background:

  • The alpha-hemolysin (alphaHL) protein pore is a versatile tool with numerous biotechnological applications.
  • Understanding single-molecule behavior is crucial for advancing molecular engineering and diagnostics.

Purpose of the Study:

  • To develop a single-molecule manipulation system utilizing the alphaHL pore's nanocavity.
  • To investigate the folding, unfolding, and translocation dynamics of thrombin-binding aptamer (TBA) G-quadruplexes within the nanocavity.

Main Methods:

  • Utilized a single-molecule manipulation system based on the alphaHL protein pore.
  • Employed noncovalent encapsulation of thrombin-binding aptamer (TBA) within the pore's nanocavity.
  • Monitored changes in pore conductance to detect molecular events and used Tag-TBA for localization.

Main Results:

  • Observed characteristic changes in pore conductance upon trapping the TBA G-quadruplex.
  • Detected spontaneous unfolding of the G-quadruplex structure and translocation of unfolded DNA.
  • Localized the G-quadruplex near the beta-barrel entry, observing molecular vibration and rotation.

Conclusions:

  • The developed guest-nanocavity supramolecular system effectively probes single-molecule dynamics.
  • This system provides insights into the folding and unfolding kinetics of G-quadruplex structures.
  • Potential applications exist for understanding complex molecular processes at the single-molecule level.