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

Channel Rhodopsins01:11

Channel Rhodopsins

Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...

You might also read

Related Articles

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

Sort by
Same author

Binding orientation of weakly associating membrane peripheral proteins via membrane paramagnetic relaxation enhancement NMR.

Communications chemistry·2026
Same author

ARF: the most misunderstood GTPase I ever knew - why study ARF GAPs.

Frontiers in molecular biosciences·2025
Same author

An active allosteric mechanism in ASAP1-mediated Arf1 GTP hydrolysis redefines PH domain function.

Nature communications·2025
Same author

Small angle neutron scattering study of rhodopsin oligomerization and G-protein coupling in a physiologically relevant lipid membrane.

Biochimica et biophysica acta. Biomembranes·2025
Same author

Redefining PH Domain Function: An Active Allosteric Mechanism in ASAP1-Mediated Arf1 GTP Hydrolysis.

Research square·2025
Same author

The PH domain in the ArfGAP ASAP1 drives catalytic activation through an unprecedented allosteric mechanism.

Research square·2025

Related Experiment Video

Updated: May 14, 2026

Methodology for Studying Interactions of Vitamin A Membrane Receptors and Opsin Protein with their Ligands in Generating the Retinylidene Protein
08:18

Methodology for Studying Interactions of Vitamin A Membrane Receptors and Opsin Protein with their Ligands in Generating the Retinylidene Protein

Published on: October 4, 2024

Rhodopsin-lipid interactions studied by NMR.

Olivier Soubias1, Klaus Gawrisch

  • 1Laboratory of Membrane Biochemistry and Biophysics, NIAAA, National Institutes of Health, Bethesda, Maryland, USA. gawrisch@helix.nih.gov

Methods in Enzymology
|February 5, 2013
PubMed
Summary

We developed a new method using anodic aluminum oxide (AAO) filters to reconstitute membrane proteins. This technique allows detailed study of how proteins like rhodopsin affect lipid bilayers, improving understanding of integral membrane protein function.

More Related Videos

A Rhodopsin Transport Assay by High-Content Imaging Analysis
12:11

A Rhodopsin Transport Assay by High-Content Imaging Analysis

Published on: January 16, 2019

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer
12:23

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer

Published on: August 20, 2012

Related Experiment Videos

Last Updated: May 14, 2026

Methodology for Studying Interactions of Vitamin A Membrane Receptors and Opsin Protein with their Ligands in Generating the Retinylidene Protein
08:18

Methodology for Studying Interactions of Vitamin A Membrane Receptors and Opsin Protein with their Ligands in Generating the Retinylidene Protein

Published on: October 4, 2024

A Rhodopsin Transport Assay by High-Content Imaging Analysis
12:11

A Rhodopsin Transport Assay by High-Content Imaging Analysis

Published on: January 16, 2019

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer
12:23

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer

Published on: August 20, 2012

Area of Science:

  • Biophysics
  • Membrane Protein Biochemistry
  • Materials Science

Background:

  • Integral membrane protein function is influenced by the surrounding lipid matrix.
  • Previous methods for protein reconstitution faced challenges in reproducibility and detergent removal.

Purpose of the Study:

  • To introduce a novel sample preparation method for reconstituting membrane proteins using anodic aluminum oxide (AAO) filters.
  • To enable high-resolution studies on the impact of protein insertion on lipid properties and lipid-protein interactions.

Main Methods:

  • Utilized porous AAO filters with 200-nm pores to create tubular, detergent-free, single lipid bilayers.
  • Employed (2)H NMR order parameter measurements and (1)H saturation-transfer NMR with magic angle spinning.
  • Reconstituted bovine rhodopsin as a model integral membrane protein.

Main Results:

  • Generated a large surface area of solid-supported lipid bilayers (approx. 500 cm²/cm²) suitable for NMR.
  • Demonstrated that rhodopsin insertion causes elastic deformation of the lipid membrane.
  • Detected specific lipid-protein interactions, indicating preferences for certain lipid species.

Conclusions:

  • The AAO filter method provides a reproducible platform for studying membrane protein biophysics.
  • Integral membrane protein function is modulated by both protein-induced membrane deformation and specific lipid-protein interactions.