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Updated: Jun 22, 2026

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
Published on: March 5, 2017
Directed formation of lipid membrane microdomains as high affinity sites for His-tagged proteins
Carl C Hayden1, Jane S Hwang, Elisa A Abate
1Sandia National Laboratories, P.O. Box 969, Livermore, California 94551, USA.
Abstract:
Lipid membranes composed of an iminodiacetic acid functionalized lipid, DSIDA, in a POPC matrix exhibited switchable properties via Cu(2+) recognition to rapidly assemble microdomains that act as high affinity sites for His-tagged proteins. The microdomains demonstrated an order of magnitude enhanced affinity for the proteins compared to homogeneously functionalized POPC membranes with Ni(2+)-NTA DOGS or Cu(2+)-DOIDA, while a rapid release and restoration of the original membrane was accomplished with micromolar concentrations of EDTA.
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