Jump to main content
Jump to site search
Access to RSC content Close the message box

Continue to access RSC content when you are not at your institution. Follow our step-by-step guide.


Issue 23, 2018
Previous Article Next Article

Determining the lipid specificity of insoluble protein transmembrane domains

Author affiliations

Abstract

While the specificity of protein–lipid interactions is a key feature in the function of biological membranes, studying the specifics of these interactions is challenging because most membrane proteins are insoluble in water due to the hydrophobic nature of their transmembrane domains (TMDs). Here, we introduce a method that overcomes this solubility limitation and identifies the affinity profile of protein TMDs to specific lipid formulations. Using 5 human TMDs as a sample group, our results demonstrate that TMDs are highly selective and that these specific lipid–TMD interactions can involve either a single lipid, or the combination of multiple lipid species.

Graphical abstract: Determining the lipid specificity of insoluble protein transmembrane domains

Back to tab navigation

Supplementary files

Article information


Submitted
26 Mar 2018
Accepted
09 Oct 2018
First published
15 Oct 2018

Lab Chip, 2018,18, 3561-3569
Article type
Paper
Author version available

Determining the lipid specificity of insoluble protein transmembrane domains

R. Ziblat, J. C. Weaver, L. R. Arriaga, S. Chong and D. A. Weitz, Lab Chip, 2018, 18, 3561
DOI: 10.1039/C8LC00311D

Social activity

Search articles by author

Spotlight

Advertisements