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: 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...
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...
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...
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...
Mass Spectrometers01:16

Mass Spectrometers

This lesson details the instrumentation of a mass spectrometer—a physical instrument to perform mass spectrometry on analyte molecules and record the characteristic mass spectra. This is achieved via three chief functions:

You might also read

Related Articles

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

Sort by
Same author

Direct Growth of Na-Ion Conducting Na<sub>3</sub>O<sub>15</sub>Si<sub>6</sub>Y Solid Glass Electrolyte With Reduced Interfacial Resistance for Safer Room-Temperature Sodium-Sulfur Pouch Cells.

Angewandte Chemie (International ed. in English)·2026
Same author

Machine learning-guided discovery of spirocyclic inhibitors targeting Mycobacterium tuberculosis FtsZ.

Folia microbiologica·2026
Same author

Tinosporide promotes melanogenesis via activation of cAMP/PKA/CREB-MITF signaling in B16F10 and SK-MEL-2 cells.

Journal of natural medicines·2026
Same author

Genomic characterization of multidrug-resistant Escherichia coli isolated from gills of Labeo rohita: Insight into resistome, virulence and pathogenicity.

PloS one·2026
Same author

Host-pathogen interplay of Orientia tsutsugamushi: pathomolecular epidemiology and phylo-immuno profiling in naturally infected rodents and shrews.

Microbial pathogenesis·2026
Same author

Cross-frequency bispectral EEG analysis of reach-to-grasp planning and execution.

Computers in biology and medicine·2026

Related Experiment Video

Updated: Jun 4, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

An efficient algorithmic approach for mass spectrometry-based disulfide connectivity determination using multi-ion

William Murad1, Rahul Singh, Ten-Yang Yen

  • 1Department of Computer Science, San Francisco State University, 1600 Holloway Avenue, San Francisco, CA 94132, USA. whemurad@sfsu.edu

BMC Bioinformatics
|February 24, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces an efficient algorithm for determining protein disulfide bond patterns using mass spectrometry. The new method accurately identifies complex disulfide bonds, improving upon existing techniques.

More Related Videos

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

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 4, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

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:

  • Proteomics
  • Computational Biology
  • Biochemistry

Background:

  • Determining protein disulfide (S-S) bond patterns is crucial for understanding protein structure and function.
  • Mass spectrometry (MS) is used for S-S bond analysis, but existing methods face algorithmic challenges in matching experimental data to potential bond structures.
  • Current approaches often simplify analysis by considering only specific ion types, potentially reducing accuracy.

Purpose of the Study:

  • To develop an efficient algorithmic approach for determining protein disulfide bond patterns from mass spectrometry data.
  • To overcome limitations of existing methods by analyzing multiple ion types and complex bonding topologies.
  • To provide a computationally efficient and accurate solution for disulfide bond determination.

Main Methods:

  • An approximation algorithm-based search formulation combined with data-driven parameter estimation.
  • Analysis of multiple ion types (a, b, bo, b*, c, x, y, yo, y*, and z) to improve accuracy.
  • Consideration of complex bonding topologies, including inter/intra-peptide bonds involving more than two peptides.
  • Global consistency checks and confidence scoring for each identified disulfide bond.

Main Results:

  • The method demonstrated high efficiency, sensitivity, specificity, and accuracy on nine eukaryotic Glycosyltransferases with varying disulfide bond complexities.
  • Performance was comparable to or better than state-of-the-art techniques.
  • The approach effectively handles complex disulfide bonding patterns.

Conclusions:

  • This research presents a novel algorithmic solution to significant challenges in MS-based disulfide bond determination.
  • It is the first algorithmic approach to consider multiple ion types while maintaining polynomial time complexity and high accuracy.
  • The developed method offers a more comprehensive and accurate tool for protein disulfide bond analysis.