Abstract
Detecting the behaviors of proteins in membranes is often challenging; we need to develop new methods to better understand the mechanisms involved. We have developed two types of peptide-based experimental systems that can detect the self-association of proteins in bilayer environments: 1) a single-pair fluorescence detection system for studying the self-association of transmembrane helices in model membranes; and 2) live-cell fluorescence labeling and analysis of the oligomeric state of membrane proteins using a coiled-coil labeling method. By using these methods, we show that membrane cholesterol significantly affects the self-association of transmembrane helices.
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