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

You might also read

Related Articles

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

Sort by
Same author

Orbitrap Collision Cross Section Measurements Enhance Isomer Annotations in Lipidomics.

bioRxiv : the preprint server for biology·2026
Same author

Revealing the Fate of Isomeric Monounsaturated Fatty Acids in <i>Enterococcus faecalis</i> Membrane Lipids and Their Influence on Antimicrobial Susceptibility.

ACS infectious diseases·2026
Same author

Design of Fluorescent Membrane Scaffold Proteins for Nanodiscs.

bioRxiv : the preprint server for biology·2026
Same author

First 20 Years of Orbitrap Mass Spectrometry as the Mainstream Analytical Technique.

Mass spectrometry reviews·2026
Same author

LetA defines a structurally distinct transporter family.

Nature·2026
Same author

Incorporation of Temperature Impact on Hot-Carrier Degradation into Compact Physics Model.

Micromachines·2025

Related Experiment Video

Updated: Feb 20, 2026

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

15.0K

Engineering Nanodisc Scaffold Proteins for Native Mass Spectrometry.

Deseree J Reid1, James E Keener1, Andrew P Wheeler1

  • 1Department of Chemistry and Biochemistry, University of Arizona , Tucson, Arizona 85721, United States.

Analytical Chemistry
|October 20, 2017
PubMed
Summary

Engineered membrane scaffold proteins (MSP) simplify native mass spectrometry of lipoprotein nanodiscs. This method allows unambiguous assignment of nanodisc spectra and protein stoichiometry, aiding membrane protein analysis.

More Related Videos

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

20.5K
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

Related Experiment Videos

Last Updated: Feb 20, 2026

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

15.0K
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

20.5K
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

Area of Science:

  • Biochemistry
  • Structural Biology
  • Analytical Chemistry

Background:

  • Lipoprotein nanodiscs offer a stable nanoscale lipid bilayer for membrane protein analysis via native mass spectrometry.
  • Native mass spectrometry of nanodiscs often yields complex spectra, hindering unambiguous interpretation and protein stoichiometry assignment.

Purpose of the Study:

  • To develop a method for simplifying and improving the interpretation of native mass spectrometry data from lipoprotein nanodiscs.
  • To enable unambiguous determination of membrane scaffold protein (MSP) stoichiometry within nanodiscs.

Main Methods:

  • Engineering of mutant membrane scaffold proteins (MSP) to controllably shift nanodisc masses.
  • Utilizing mixed belt assemblies of MSP variants to encode stoichiometry in spectral peak shapes.
  • Applying native mass spectrometry to analyze engineered nanodiscs with embedded membrane proteins.

Main Results:

  • Mutant MSPs enabled controllable mass shifts in nanodiscs, eliminating isobaric interference from lipids.
  • Mixing different MSP belts allowed unambiguous assignment of MSP stoichiometry directly from mass spectra.
  • Demonstrated confirmation of MSP dissociation prior to desolvation using mixed belt nanodiscs.

Conclusions:

  • Engineered MSPs provide a powerful tool for simplifying and enhancing native mass spectrometry of lipoprotein nanodiscs.
  • The developed method facilitates unambiguous spectral interpretation and stoichiometry determination for membrane protein studies.
  • This approach aids in understanding membrane protein behavior and interactions within a native-like lipid environment.