Related Experiment Video
Updated: Aug 6, 2026

A Rhodopsin Transport Assay by High-Content Imaging Analysis
Published on: January 16, 2019
Sulfhydryl group modification of photoreceptor G-protein prevents its light-induced binding to rhodopsin
Abstract:
The effect of sulfhydryl modification on the light-induced interaction between rhodopsin and the peripheral GTP-binding protein of the photoreceptor membrane (G-protein) has been investigated by time-resolved near-infrared light-scattering and polyacrylamide gel electrophoresis. It has been found that the modification of rhodopsin with the alkylating agent N-ethylmaleimide (NEM) does not affect its light-induced interaction with the G-protein. Modification of G-protein with NEM or other sulfhydryl agents prevents any light-induced binding to rhodopsin. Dark-association of G to the membrane as well as the light-induced complex with rhodopsin (once formed) is insensitive to NEM.
More Related Videos
09:19Strategic Screening and Characterization of the Visual GPCR-mini-G Protein Signaling Complex for Successful Crystallization
Published on: March 16, 2020
11:08Two Peeling Methods for the Isolation of Photoreceptor Cell Compartments in the Mouse Retina for Protein Analysis
Published on: December 7, 2021
Related Concept Videos
Photoreceptors and Plant Responses to Light
Channel Rhodopsins
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
Activation and Inactivation of G Proteins
GPCR Desensitization
G-Protein Gated Ion Channels
Sensory organs,...
Photoreceptors and Visual Pathways