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

Two-dimensional Gel Electrophoresis01:22

Two-dimensional Gel Electrophoresis

Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as  cells...
Electrophoresis: Overview01:20

Electrophoresis: Overview

Electrophoresis is a powerful analytical separation technique that relies on the differential migration of charged species when subjected to an electric field. The core strength of electrophoresis lies in its ability to separate high-molecular-weight species in complex mixtures. It has found widespread use in biochemistry, molecular biology, and analytical chemistry, allowing the separation of compounds like amino acids, nucleotides, carbohydrates, and proteins with excellent resolution.
There...
SDS-PAGE01:27

SDS-PAGE

Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed  polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
Globular Proteins01:27

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
Capillary Electrophoresis: Applications01:30

Capillary Electrophoresis: Applications

Capillary electrophoretic separations offer various modes, each with unique applications. These modes include capillary zone electrophoresis, capillary gel electrophoresis, capillary array electrophoresis, capillary isoelectric focusing, capillary isotachophoresis, micellar electrokinetic chromatography, and capillary electrochromatography.
Capillary zone electrophoresis (CZE) separates ionic components based on their electrophoretic mobility. It has been used to separate proteins, amino acids,...

You might also read

Related Articles

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

Sort by
Same author

Clustering of PCOS-like traits in naturally hyperandrogenic female rhesus monkeys.

Human reproduction (Oxford, England)·2017
Same author

Use of opportunistic clinical data and a population pharmacokinetic model to support dosing of clindamycin for premature infants to adolescents.

Clinical pharmacology and therapeutics·2014
Same author

Transposable elements donate lineage-specific regulatory sequences to host genomes.

Cytogenetic and genome research·2005
Same author

Charge-reduced nano electrospray ionization combined with differential mobility analysis of peptides, proteins, glycoproteins, noncovalent protein complexes and viruses.

Journal of mass spectrometry : JMS·2001
Same author

Retinoid metabolism in the prostate: effects of administration of the synthetic retinoid N-(4-hydroxyphenyl)retinamide.

Cancer research·1999
Same author

Nanoparticle detection technology for chemical analysis.

Analytical chemistry·1999

Related Experiment Video

Updated: Jun 1, 2026

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)
10:00

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)

Published on: June 20, 2019

Macromolecule analysis based on electrophoretic mobility in air:  globular proteins.

S L Kaufman1, J W Skogen, F D Dorman

  • 1TSI Incorporated, 500 Cardigan Road, St. Paul, Minnesota 55126.

Analytical Chemistry
|May 31, 2011
PubMed
Summary

This study presents an aerosol-based method for analyzing globular proteins by measuring their electrophoretic mobility. The technique effectively separates proteins by size, offering a novel approach for protein characterization.

More Related Videos

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

Proteomic Profiling of Macrophages by 2D Electrophoresis
07:53

Proteomic Profiling of Macrophages by 2D Electrophoresis

Published on: November 4, 2014

Related Experiment Videos

Last Updated: Jun 1, 2026

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)
10:00

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)

Published on: June 20, 2019

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

Proteomic Profiling of Macrophages by 2D Electrophoresis
07:53

Proteomic Profiling of Macrophages by 2D Electrophoresis

Published on: November 4, 2014

Area of Science:

  • Analytical Chemistry
  • Biophysics
  • Aerosol Science

Background:

  • Characterizing globular proteins is crucial for understanding biological functions.
  • Existing methods for protein analysis can be complex and time-consuming.
  • Aerosol-based techniques offer potential for rapid, sensitive measurements.

Purpose of the Study:

  • To develop and validate an aerosol technique for separating and analyzing globular proteins.
  • To determine the feasibility of using electrophoretic mobility in air for protein mass determination.
  • To establish a method for characterizing proteins across a wide molecular mass range.

Main Methods:

  • Proteins were analyzed using an aerosol technique based on electrophoretic mobility of singly-charged molecular ions in air.
  • Ions were generated via electrospraying and drying of protein suspensions.
  • Electrophoretic mobility was measured using a modified differential mobility analyzer near atmospheric pressure.

Main Results:

  • The technique successfully separated globular proteins with molecular masses from 5.7 to 669 kDa.
  • Results were expressed as electrophoretic mobility equivalent diameters using the Millikan formula.
  • Analyzed protein concentrations ranged from 0.02 to 200 μg/mL with a 3-minute sampling time.

Conclusions:

  • The developed aerosol technique provides an effective means for separating and analyzing globular proteins.
  • This method offers a novel approach for rapid protein characterization based on size.
  • The technique demonstrates potential for broader applications in biophysical and biochemical analyses.