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...
Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

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...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Protein Networks02:26

Protein Networks

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,...

You might also read

Related Articles

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

Sort by
Same author

The Effect of a Novel Antibody-based Drug, Prospekta, on Brain Electrical Activity in Mice.

CNS & neurological disorders drug targets·2026
Same author

Editorial: Ubiquitin proteasome system (UPS) and ubiquitin-independent proteasome-mediated proteolysis (UIPP) crosstalk in development and disease.

Frontiers in cell and developmental biology·2025
Same author

Cleaving Expectations: A Review of Proteasome Functional and Catalytic Diversity.

Biomolecules·2025
Same author

Merging different allosteric mechanisms: The case of <i>Escherichia coli</i> glutathione reductase.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

A syringe-based digital algometer with a USB interface: a low-cost alternative to commercially available devices.

Frontiers in pain research (Lausanne, Switzerland)·2025
Same author

Distinct Brain Electrical Activity Patterns in Dominant and Submissive Mice: Implications for Cognitive Impairments.

The European journal of neuroscience·2025
Same journal

A Video Protocol of a Randomized Controlled Clinical Trial - Electrochemotherapy of Cutaneous Metastases with Reduced Dose Bleomycin (BLESS Trial).

Journal of visualized experiments : JoVE·2026
Same journal

A Standardized Ex Vivo Porcine Oromucosal Model for Evaluating Peptide Fluxes.

Journal of visualized experiments : JoVE·2026
Same journal

Lightweight English Text Classification with Deep Learning Based on Complex System Theory.

Journal of visualized experiments : JoVE·2026
Same journal

Integrating Artificial Intelligence-Assisted Translation Support into English Courses: Effects on Translation Accuracy, Perceived Stress, and Anxiety.

Journal of visualized experiments : JoVE·2026
Same journal

A Toxin-Based Counter-Selection System for Markerless Gene Deletion and High-Density Tn5 Transposon Mutagenesis in Pectobacterium brasiliense.

Journal of visualized experiments : JoVE·2026
Same journal

Seamless Multimodal Human-Robot Communication: Integration Techniques in Human-Computer Interaction.

Journal of visualized experiments : JoVE·2026
See all related articles

Related Experiment Video

Updated: Jun 12, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Analyzing large protein complexes by structural mass spectrometry.

Noam Kirshenbaum1, Izhak Michaelevski, Michal Sharon

  • 1Department of Biological Chemistry, Weizmann Institute of Science.

Journal of Visualized Experiments : Jove
|June 23, 2010
PubMed
Summary
This summary is machine-generated.

Structural mass spectrometry (MS) offers a powerful method for analyzing complex protein assemblies. This protocol details essential MS techniques for studying protein complexes, providing researchers with foundational knowledge for structural investigations.

More Related Videos

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Related Experiment Videos

Last Updated: Jun 12, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Area of Science:

  • Structural biology
  • Biochemistry
  • Analytical chemistry

Background:

  • Cellular processes rely on dynamic multi-protein complexes.
  • Characterizing these complexes is challenging due to heterogeneity, asymmetry, and dynamics.
  • New methods are needed to study protein organization at the tertiary level.

Purpose of the Study:

  • To provide a detailed protocol for applying structural mass spectrometry (MS) to analyze large protein assemblies.
  • To introduce researchers to the principal experimental tools and procedures for MS and MS/MS experiments on non-covalent complexes.
  • To enable the study of protein complex composition, stoichiometry, and structural topology.

Main Methods:

  • Preparation of gold-coated capillaries for nanoflow electrospray ionization (nESI).
  • Sample preparation with buffer optimization for nESI compatibility and complex integrity.
  • Step-by-step optimization of experimental conditions for high mass measurements and MS/MS data acquisition.
  • Data processing and analysis procedures.

Main Results:

  • Demonstration of a detailed protocol for structural MS analysis of protein assemblies.
  • Guidance on optimizing nESI conditions for intact complex analysis.
  • Introduction to MS and MS/MS data acquisition and interpretation for non-covalent complexes.

Conclusions:

  • Structural MS is a sensitive and rapid technique for analyzing protein complexes at endogenous levels.
  • This protocol equips researchers with fundamental MS procedures for studying protein assembly structure and function.
  • The method facilitates mechanistic understanding of cellular processes by characterizing protein complex organization.