Related Experiment Video
Updated: Jan 31, 2026

Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy
Published on: November 20, 2021
Probing Colocalization of N-Ras and K-Ras4B Lipoproteins in Model Biomembranes
Lei Li1,2, Mridula Dwivedi1, Satyajit Patra1
1Faculty of Chemistry and Chemical Biology, Physical Chemistry I, Technical University of Dortmund, Otto-Hahn-Strasse 4a, 44227, Dortmund, Germany.
Abstract:
Signaling of N-Ras and K-Ras4B proteins depends strongly on their correct localization in the cell membrane. In vivo studies suggest that intermolecular interactions foster the self-association of both N-Ras and K-Ras4B and the formation of nanoclusters in the cell membrane. As sites for effector binding, nanocluster formation is thought to be essential for effective signal transmission of both N-Ras and K-Ras4B. To shed more light on the spatial arrangement and mechanism underlying the proposed cross-talk between spatially segregated Ras proteins, the simultaneous localization of N-Ras and K-Ras4B and their effect on the lateral organization of a heterogeneous model biomembrane has been studied by using AFM and FRET methodology. It is shown that, owing to the different natures of their membrane anchor systems, N-Ras and K-Ras4B not only avoid assembly in bulk solution and do not colocalize, but rather form individual nanoclusters that diffuse independently in the fluid membrane plane.
Related Concept Videos
The Ras Gene
Ras is a...
Small GTPases - Ras and Rho
Three regulatory proteins control their activity:
Labeling DNA Probes
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...
Molecular Models
The Bohr Model
Stereotype Content Model

