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

The Equilibrium Binding Constant and Binding Strength

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

The Equilibrium Binding Constant and Binding Strength

The Equilibrium Binding Constant and Binding Strength

Electro-mechanical Systems

Electro-mechanical Systems

Electromechanical systems are intricate configurations that effectively combine electrical and mechanical elements to achieve a desired outcome. Central to many of these systems is the DC motor, a device that converts electrical energy into mechanical motion, enabling various applications ranging from simple fans to complex robotic mechanisms.
A key component of the DC motor is the armature, a rotating circuit positioned within a magnetic field. As an electric current passes through the...

Ligand Binding Sites

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

Ligand Binding and Linkage

Ligand Binding and Linkage

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...

Molecules and Compounds

Molecules and Compounds

Atoms and Molecules

You might also read

Related Articles

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

Sort by

Same author

Tracking Gene Expression of Single Mitochondria in Live Neurons Using Nanotweezers.

Journal of the American Chemical Society·2026

Same author

Machine Learning-Driven Nanopore Sensing for Quantitative, Label-Free miRNA Detection.

Small methods·2026

Same author

Single-molecule quantum tunnelling sensors.

Chemical Society reviews·2025

Same author

Delivery of Biomolecules into Individual Cells and Subcellular Compartments by Localized Electroporation via Nanopipette.

ACS nanoscience Au·2025

Same author

Spatial and Temporal Single-Cell Profiling of RNA Compartmentalization in Neurons with Nanotweezers.

ACS nano·2025

Same author

Quantum Mechanical Tunnelling Probes with Redox Cycling for Ultra-Sensitive Detection of Biomolecules.

Angewandte Chemie (International ed. in English)·2025

Same journal

Kat5 deficiency in alveolar type II cells licenses STAT6-driven glycolytic reprogramming and pulmonary fibrosis.

Nature communications·2026

Same journal

Continuous nonthermal slab gap formed by progressive tearing beneath Northeast Asia.

Nature communications·2026

Same journal

Zeolitic isolated protonic acid sites-mediated NH<sub>3</sub> storage for robust NO<sub>x</sub> removal.

Nature communications·2026

Same journal

Coaxially nested component with asymmetric fiber resonant cavity and separation membrane for gaseous and dissolved gases detection.

Nature communications·2026

Same journal

Near-unity charge readout signal in a nonlinear resonator without matching the sensor dissipation.

Nature communications·2026

Same journal

Prokaryotic Schlafen proteins cleave tRNAs during type III CRISPR immunity.

Nature communications·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jan 26, 2026

Fine-tuning the Size and Minimizing the Noise of Solid-state Nanopores

Fine-tuning the Size and Minimizing the Noise of Solid-state Nanopores

Published on: October 31, 2013

Small molecule electro-optical binding assay using nanopores.

Shenglin Cai¹, Jasmine Y Y Sze², Aleksandar P Ivanov¹

¹Department of Chemistry, Imperial College London, Exhibition Road, London, SW7 2AZ, UK.

Nature Communications

|April 19, 2019

Summary

This summary is machine-generated.

This study introduces a novel nanopore sensing method combining electrical and fluorescence detection for highly selective single-molecule analysis. This technique enables label-free detection of analytes in complex biological samples like serum and urine.

More Related Videos

Sequencing of mRNA from Whole Blood using Nanopore Sequencing

Sequencing of mRNA from Whole Blood using Nanopore Sequencing

Published on: June 3, 2019

Label-free Single Molecule Detection Using Microtoroid Optical Resonators

Label-free Single Molecule Detection Using Microtoroid Optical Resonators

Published on: December 29, 2015

Related Experiment Videos

Last Updated: Jan 26, 2026

Fine-tuning the Size and Minimizing the Noise of Solid-state Nanopores

Fine-tuning the Size and Minimizing the Noise of Solid-state Nanopores

Published on: October 31, 2013

Sequencing of mRNA from Whole Blood using Nanopore Sequencing

Sequencing of mRNA from Whole Blood using Nanopore Sequencing

Published on: June 3, 2019

Label-free Single Molecule Detection Using Microtoroid Optical Resonators

Label-free Single Molecule Detection Using Microtoroid Optical Resonators

Published on: December 29, 2015

Area of Science:

Biotechnology
Nanotechnology
Analytical Chemistry

Background:

Single-molecule detection of nucleic acids and proteins is crucial for developing new diagnostic tools.
Nanopore sensing offers label-free, single-molecule sensitivity but struggles with selectivity for small molecules.
Current methods often require direct analyte labeling, limiting their application in complex biological fluids.

Purpose of the Study:

To develop a hybrid nanopore sensing strategy integrating electrical and fluorescence detection for enhanced molecular selectivity.
To demonstrate the capability of this method for label-free, single-molecule binding assays.
To assess the potential of this approach for analyzing targets in complex biological samples.

Main Methods:

Grafting molecular beacons, complementary DNA, or proteins onto a DNA molecular carrier for selective analyte capture.
Utilizing a nanopore setup that combines electrical signal transduction with fluorescence-based detection.
Analyzing the fraction of synchronized electrical and optical events to identify specific binding interactions.

Main Results:

Demonstrated successful detection of analytes through synchronized electrical and optical signals in a nanopore.
Achieved selective single-molecule binding assays without direct analyte labeling.
Validated the method's applicability in complex biological matrices, including human serum and urine.

Conclusions:

The hybrid nanopore sensing approach significantly improves selectivity for single-molecule detection.
This label-free strategy holds promise for analyzing targets in challenging biological samples.
Future optimization could lead to next-generation clinical assays for protein quantification and gene mutation analysis.