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

Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
Measuring Reaction Rates03:09

Measuring Reaction Rates

Polarimetry finds application in chemical kinetics to measure the concentration and reaction kinetics of optically active substances during a chemical reaction. Optically active substances have the capability of rotating the plane of polarization of linearly polarized light passing through them—a feature called optical rotation. Optical activity is attributed to the molecular structure of substances. Normal monochromatic light is unpolarized and possesses oscillations of the electrical field in...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
Fast Reactions01:27

Fast Reactions

Fast reactions occurring in times shorter than the time needed to mix reactants pose a unique challenge for investigation. In a liquid-phase continuous-flow system, reactants A and B are swiftly pushed into the mixing chamber, where mixing occurs within 1 ms. The reaction mixture then flows through an observation tube, and one measures light absorption to determine species concentrations at various points of the tube. This method is most appropriate when relatively large volumes of reactants...

You might also read

Related Articles

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

Sort by
Same author

Temperature and lipid composition differentially regulate KRAS assemblies on membranes.

Chemical communications (Cambridge, England)·2026
Same author

Peptidomimetic α,β-Unsaturated Ethyl Esters Are Irreversible Inactivators of Human Cathepsin L and Are Potent Inhibitors of SARS-CoV-2 in Cellular Models of COVID-19.

Journal of medicinal chemistry·2026
Same author

Rubisco kinetic acclimation at the holoenzyme level.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

From vibrations to function: Spectroscopic detection and quantification of π-π stacking in drug-responsive protein complexes.

Science advances·2026
Same author

Screening pertactin-specific antibodies and evaluating competitive epitope recognition by native mass spectrometry.

Chemical science·2026
Same author

IscS Kinetics in Native Mass Spectrometry Buffers Reveal Key Physiochemical Properties that Influence Enzyme Activity.

Journal of the American Society for Mass Spectrometry·2025
Same journal

Carbonylative Aminative Suzuki-Miyaura Coupling: Pd-Catalyzed Synthesis of Amides from Vinyl/Aryl Halides and Boronic Acids.

Journal of the American Chemical Society·2026
Same journal

Divergent Asymmetric Synthesis of Glutinosasins A-E.

Journal of the American Chemical Society·2026
Same journal

Ultrastrong Polyketone Hot-Melt Adhesives Enabled by Ni-Catalyzed Carbonylative Polymerization.

Journal of the American Chemical Society·2026
Same journal

Programmable Anomalous Photovoltaics Enabled by Light-Electric Dual-Field Control.

Journal of the American Chemical Society·2026
Same journal

Biomimetic Redox-Mediated Proton Relay in Nanoreactors for Photocatalysis.

Journal of the American Chemical Society·2026
Same journal

The Sulfur Monoxide-Water Complex.

Journal of the American Chemical Society·2026
See all related articles

Related Experiment Video

Updated: May 11, 2026

Mass-Sensitive Particle Tracking to Characterize Membrane-Associated Macromolecule Dynamics
13:30

Mass-Sensitive Particle Tracking to Characterize Membrane-Associated Macromolecule Dynamics

Published on: February 18, 2022

Time-Resolved Native Mass Spectrometry for Direct Measurement of Biomolecular Kinetics.

Virginia K James1, Lauren Stover1, Hanieh Bahramimoghaddam1

  • 1Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States.

Journal of the American Chemical Society
|May 9, 2026
PubMed
Summary
This summary is machine-generated.

This study introduces time-resolved native mass spectrometry (MS) for direct, label-free kinetic analysis of biomolecular interactions. This new method quantifies binding kinetics rapidly using minimal sample amounts.

More Related Videos

Real-Time Metabolic Detection in Living Cells Using Hyperpolarized 13C NMR
09:05

Real-Time Metabolic Detection in Living Cells Using Hyperpolarized 13C NMR

Published on: July 8, 2025

Improved Polymerase Chain Reaction-restriction Fragment Length Polymorphism Genotyping of Toxic Pufferfish by Liquid Chromatography/Mass Spectrometry
09:34

Improved Polymerase Chain Reaction-restriction Fragment Length Polymorphism Genotyping of Toxic Pufferfish by Liquid Chromatography/Mass Spectrometry

Published on: September 20, 2016

Related Experiment Videos

Last Updated: May 11, 2026

Mass-Sensitive Particle Tracking to Characterize Membrane-Associated Macromolecule Dynamics
13:30

Mass-Sensitive Particle Tracking to Characterize Membrane-Associated Macromolecule Dynamics

Published on: February 18, 2022

Real-Time Metabolic Detection in Living Cells Using Hyperpolarized 13C NMR
09:05

Real-Time Metabolic Detection in Living Cells Using Hyperpolarized 13C NMR

Published on: July 8, 2025

Improved Polymerase Chain Reaction-restriction Fragment Length Polymorphism Genotyping of Toxic Pufferfish by Liquid Chromatography/Mass Spectrometry
09:34

Improved Polymerase Chain Reaction-restriction Fragment Length Polymorphism Genotyping of Toxic Pufferfish by Liquid Chromatography/Mass Spectrometry

Published on: September 20, 2016

Area of Science:

  • Biochemistry
  • Biophysics
  • Analytical Chemistry

Background:

  • Biomolecular interaction kinetics are crucial for understanding biological processes and drug action.
  • Conventional methods like surface plasmon resonance and biolayer interferometry (BLI) have limitations, including the need for immobilization or labeling and indirect measurements.

Purpose of the Study:

  • To develop a direct, label-free, and immobilization-free method for quantifying biomolecular kinetics.
  • To overcome limitations of existing kinetic assays and enhance the utility of native mass spectrometry (MS).

Main Methods:

  • Development and application of time-resolved native mass spectrometry (MS).
  • Direct, label-free, and immobilization-free quantification of biomolecular association and dissociation kinetics.
  • Utilizing picomolar sample amounts for rapid kinetic measurements.

Main Results:

  • The time-resolved native MS approach provides direct kinetic parameter quantification.
  • Results were benchmarked against BLI, showing agreement in kinetic parameters.
  • Successfully quantified kinetics of protein-small-molecule interactions, including irreversible inhibitors.

Conclusions:

  • Time-resolved native MS transforms native MS into a dynamic tool for quantitative kinetic analysis.
  • This method offers a powerful new approach for studying biomolecular interactions and mechanisms in therapeutic discovery.
  • Overcomes longstanding limitations of conventional kinetic assays, enabling faster and more direct measurements.