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 Analyzers: Overview01:13

Mass Analyzers: Overview

1.9K
The mass analyzer is a crucial component of the mass spectrometer. In the ionization chamber, the vaporized sample is bombarded with a high-energy electron beam to generate a radical cation and further fragment into neutral molecules, radicals, and cations. A series of negatively charged accelerator plates accelerate the cations into the mass analyzer. The mass analyzer separates ions according to their mass-to-charge (m/z) ratios and then directs them to the detector. The common types of mass...
1.9K

You might also read

Related Articles

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

Sort by
Same author

Measuring nanoparticles in the size range to 2000 nm.

Journal of nanoparticle research : an interdisciplinary forum for nanoscale science and technology·2019
See all related articles

Related Experiment Video

Updated: Feb 23, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

24.9K

Measuring proteins with greater speed and resolution while reducing sample size.

Vincent H Hsieh1, Philip J Wyatt2

  • 1Wyatt Technology Corporation, 6330 Hollister Avenue, Goleta, California, 93117, USA. vhsieh@wyatt.com.

Scientific Reports
|September 1, 2017
PubMed
Summary

A new multi-angle light scattering (MALS) method offers faster, high-resolution measurement of protein mass and size. This breakthrough enhances biomolecular characterization and biologics development, requiring less sample.

More Related Videos

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor
09:49

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Published on: April 6, 2016

8.5K
Digital Microfluidics for Automated Proteomic Processing
10:55

Digital Microfluidics for Automated Proteomic Processing

Published on: November 6, 2009

13.1K

Related Experiment Videos

Last Updated: Feb 23, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

24.9K
Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor
09:49

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Published on: April 6, 2016

8.5K
Digital Microfluidics for Automated Proteomic Processing
10:55

Digital Microfluidics for Automated Proteomic Processing

Published on: November 6, 2009

13.1K

Area of Science:

  • Biochemistry and Biophysics
  • Analytical Chemistry
  • Biotechnology

Background:

  • Accurate macromolecular characterization is vital for biologics development.
  • Existing multi-angle light scattering (MALS) methods face limitations with small sample volumes.
  • Standardized protein reference materials are crucial for technique validation.

Purpose of the Study:

  • To introduce a novel MALS methodology overcoming microliter-scale peak volume limitations.
  • To demonstrate enhanced resolution and signal-to-noise performance in MALS measurements.
  • To showcase the system's capability using a new NIST protein standard (SRM 8671).

Main Methods:

  • Development of a new multi-angle light scattering (MALS) system.
  • Integration of MALS with chromatographic separation.
  • Simultaneous online dynamic light scattering (DLS) measurements.
  • Utilizing NIST SRM 8671 for system validation.

Main Results:

  • Achieved highest resolution and signal-to-noise performance in MALS.
  • Successfully measured sharp chromatography peaks (20-25 µL FWHM) with high precision.
  • Demonstrated 10x faster protein mass and size measurements compared to previous methods.
  • Reduced sample requirements for precise macromolecular analysis.

Conclusions:

  • The new MALS methodology significantly advances macromolecular characterization capabilities.
  • This system offers rapid, high-resolution analysis essential for biologics and bio-therapeutic development.
  • The technology promises broad impact across research, production, and quality control stages.