Related Experiment Video
Updated: Aug 10, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
Conformational change of bacteriorhodopsin quantitatively monitored by microcantilever sensors
Thomas Braun1, Natalija Backmann, Manuel Vögtli
1National Center of Competence for Research in Nanoscale Science, Institute of Physics, and Maurice E. Müller Institute, Biozentrum, University of Basel, 4056 Basel, Switzerland.
Abstract:
Bacteriorhodopsin proteoliposomes were used as a model system to explore the applicability of micromechanical cantilever arrays to detect conformational changes in membrane protein patches. The three main results of our study concern: 1), reliable functionalization of micromechanical cantilever arrays with proteoliposomes using ink jet spotting; 2), successful detection of the prosthetic retinal removal (bleaching) from the bacteriorhodopsin protein by measuring the induced nanomechanical surface stress change; and 3), the quantitative response thereof, which depends linearly on the amount of removed retinal. Our results show this technique to be a potential tool to measure membrane protein-based receptor-ligand interactions and conformational changes.
More Related Videos
10:03Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
14:13Atomic Force Microscopy of Red-Light Photoreceptors Using PeakForce Quantitative Nanomechanical Property Mapping
Published on: October 24, 2014