Issue 17, 2015

A review of traditional and emerging methods to characterize lipid–protein interactions in biological membranes

Abstract

Current understanding of the cell membrane suggests that it is a patchwork structure composed of many proteins and lipids that are not all freely diffusing, but rather can take part in dynamic microdomains within the plane of the membrane. These domains can form or be maintained in several ways, such as “lipid shells” around proteins and/or cytoskeletal compartmentalization. Interactions within a micro-environment not only co-localize multiple components of some functional unit, but also may be involved in the regulation of that unit's activity. However, studies of protein–lipid associations and their impacts on protein activity are challenging for a number of reasons. In this review we describe the salient features of classical and emerging methodologies for studying protein–lipid interactions and their limitations.

Graphical abstract: A review of traditional and emerging methods to characterize lipid–protein interactions in biological membranes

Article information

Article type
Tutorial Review
Submitted
06 3 2015
Accepted
18 4 2015
First published
20 4 2015

Anal. Methods, 2015,7, 7076-7094

A review of traditional and emerging methods to characterize lipid–protein interactions in biological membranes

C. Hsia, M. J. Richards and S. Daniel, Anal. Methods, 2015, 7, 7076 DOI: 10.1039/C5AY00599J

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements