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

Mass Spectrometry of Amines01:15

Mass Spectrometry of Amines

5.4K
In mass spectroscopy, amines undergo fragmentation to give parent ions with odd molecule weights. This observed mass spectrum follows the nitrogen rule; a molecule with an odd number of nitrogen atoms produces a molecular ion with an odd molecular weight. Amines undergo fragmentation through α cleavage, producing nitrogen-containing cations—iminium ions—and alkyl radicals. Mass spectra of aromatic and cyclic aliphatic amines exhibit strong molecular ion peaks, but acyclic...
5.4K
Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

9.0K
Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
9.0K
Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

4.3K
Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...
4.3K
Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

2.5K
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...
2.5K
Chemical Ionization (CI) Mass Spectrometry01:21

Chemical Ionization (CI) Mass Spectrometry

1.6K
The molecular ion peak of a molecule in the mass spectrum provides vital information for molecular identification. However, conventional electron impact ionization can lead to the rapid dissociation of some molecular ions before they reach the detector. A milder ionization method is required to increase the lifetime of such ionized analyte molecules. Chemical ionization (CI) is a gas-phase protonation reaction useful for mass-analyzing analyte molecules that are easily protonated to yield the...
1.6K
Mass Spectrometry: Alkene Fragmentation00:59

Mass Spectrometry: Alkene Fragmentation

3.7K
Alkenes lose one electron from the unsaturated π bond upon ionization and form stable molecular ions. Further fragmentation of alkenes occurs through three different reaction pathways. The most prominent fragmentation is the cleavage at the allylic position. The resultant allylic carbocation is resonance stabilized. In the mass spectra of terminal alkenes, this fragment appears at a mass-to-charge ratio of 41. In the internal alkenes, where there are two choices of allylic cleavage, the...
3.7K

You might also read

Related Articles

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

Sort by
Same author

Attention based residual network for medicinal fungi near infrared spectroscopy analysis.

Mathematical biosciences and engineering : MBE·2019
Same author

Trimetazidine attenuates high-altitude fatigue and cardiorespiratory fitness impairment: A randomized double-blinded placebo-controlled clinical trial.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2019
Same author

TNF-α-induced Tim-3 expression marks the dysfunction of infiltrating natural killer cells in human esophageal cancer.

Journal of translational medicine·2019
Same author

First Community-Wide, Comparative Cross-Linking Mass Spectrometry Study.

Analytical chemistry·2019
Same author

In vivo assembly and trafficking of olfactory Ionotropic Receptors.

BMC biology·2019
Same author

Plinabulin, an inhibitor of tubulin polymerization, targets KRAS signaling through disruption of endosomal recycling.

Biomedical reports·2019
Same journal

Tracking Synthetic Adhesins on Bacterial Surfaces with Immunofluorescence Microscopy.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Post-Selection Methods for Analyzing mRNA Display Selections and Optimization of Hits.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

High-Performance Computing in Tandem Mass Spectrometry (MS/MS) Peptide Identification.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Engineering and Adapting Disulfide-Containing Proteins to Enable Intracellular Functionality.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

AI-Driven Protein Research: From Prediction to Design.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Methods for the In Vitro Selection of Protein and Peptide Libraries Using mRNA Display.

Methods in molecular biology (Clifton, N.J.)·2026
See all related articles

Related Experiment Video

Updated: Feb 9, 2026

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
09:18

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

10.3K

Defining dynamic protein interactions using SILAC-based quantitative mass spectrometry.

Xiaorong Wang1, Lan Huang

  • 1Department of Physiology & Biophysics, University of California, Irvine, Medical Science I, D233, 160 Aldrich Hall, Irvine, CA, 92697, USA.

Methods in Molecular Biology (Clifton, N.J.)
|July 26, 2014
PubMed
Summary
This summary is machine-generated.

This study introduces advanced methods for identifying dynamic protein-protein interactions, crucial for understanding cellular functions. The approach combines innovative sample preparation with quantitative mass spectrometry for precise analysis.

More Related Videos

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics
12:53

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Published on: July 6, 2014

32.0K
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

19.0K

Related Experiment Videos

Last Updated: Feb 9, 2026

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
09:18

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

10.3K
Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics
12:53

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Published on: July 6, 2014

32.0K
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

19.0K

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Proteomics

Background:

  • Protein-protein interactions are fundamental to cellular processes.
  • Understanding these interactions is key to deciphering protein function regulation.
  • Current methods struggle to identify dynamic protein interactors.

Purpose of the Study:

  • To develop integrated strategies for identifying dynamic protein interactors.
  • To enhance the systematic study of protein-protein interactions.
  • To improve the characterization of protein complex dynamics.

Main Methods:

  • Affinity purification coupled with mass spectrometry (AP-MS).
  • Quantitative mass spectrometry for distinguishing specific from nonspecific interactions.
  • Stable Isotope Labeling by Amino acids in Cell culture (SILAC)-based quantitation.
  • Novel sample preparation techniques.

Main Results:

  • The integrated strategies enable efficient identification of dynamic interactors.
  • Quantitative mass spectrometry effectively differentiates specific binding partners.
  • The methods capture interactions missed by standard biochemical techniques.

Conclusions:

  • The described integrated strategies significantly advance the study of dynamic protein interactions.
  • This approach provides a more comprehensive understanding of protein complex behavior.
  • The methods are essential for a complete characterization of protein-protein interaction networks.