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

Mass Spectrometry: Complex Analysis

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 Spectrometry

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...

Tandem Mass Spectrometry

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...

You might also read

Related Articles

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

Sort by

Same author

OBP2A regulates epidermal barrier function and protects against cytotoxic small hydrophobic molecules.

iScience·2024

Same author

A mechanism of melanogenesis mediated by E-cadherin downregulation and its involvement in solar lentigines.

International journal of cosmetic science·2023

Same author

Oral Supplementation of Collagen Peptides Improves Skin Hydration by Increasing the Natural Moisturizing Factor Content in the Stratum Corneum: A Randomized, Double-Blind, Placebo-Controlled Clinical Trial.

Skin pharmacology and physiology·2021

Same author

Influence of hydrophilic additives on the signal intensity in electrospray ionization of flavonoid glycosides.

Rapid communications in mass spectrometry : RCM·2020

Same author

Influence of Solvent Composition and Surface Tension on the Signal Intensity of Amino Acids in Electrospray Ionization Mass Spectrometry.

Mass spectrometry (Tokyo, Japan)·2020

Same author

Key component of inflammasome, NLRC4, was identified in the lesional epidermis of psoriatic patients.

The Journal of dermatology·2018

Search research articles

Related Experiment Video

Updated: Jun 29, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Multidimensional LC separations in shotgun proteomics.

Akira Motoyama¹, John R Yates

¹Shiseido Co.

Analytical Chemistry

|October 2, 2008

Summary

This summary is machine-generated.

Researchers can study complex biological structures using mass spectrometry (MS) coupled with two separation modes. This advanced technique enhances the analysis of intricate biological samples.

More Related Videos

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Related Experiment Videos

Last Updated: Jun 29, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Area of Science:

Biochemistry
Analytical Chemistry
Molecular Biology

Background:

Studying complex biological structures is crucial for understanding cellular functions.
Traditional analytical methods often struggle with the complexity of biological samples.

Purpose of the Study:

To introduce and validate a novel analytical approach for studying complex biological structures.
To demonstrate the advantages of combining multiple separation techniques with mass spectrometry.

Main Methods:

Utilized two distinct separation modes prior to mass spectrometry analysis.
Employed advanced mass spectrometry (MS) for high-resolution detection and identification.
Applied the coupled separation-MS technique to analyze intricate biological samples.

Main Results:

Successfully resolved and identified components within complex biological mixtures.
Demonstrated enhanced sensitivity and specificity compared to single separation methods.
Provided detailed insights into the composition of biological structures.

Conclusions:

The combination of dual separation modes with MS is a powerful strategy for analyzing complex biological systems.
This approach significantly advances the capability to investigate intricate biological structures.
Offers a robust platform for future discoveries in molecular biology and biochemistry.