| Literature DB >> 34346484 |
Alyssa E Ward1, Yujie Ye1, Jennifer A Schuster1, Shushu Wei1, Francisco N Barrera1.
Abstract
The study of membrane proteins is undergoing a golden era, and we are gaining unprecedented knowledge on how this key group of proteins works. However, we still have only a basic understanding of how the chemical composition and the physical properties of lipid bilayers control the activity of membrane proteins. Single-molecule (SM) fluorescence methods can resolve sample heterogeneity, allowing to discriminate between the different molecular populations that biological systems often adopt. This short review highlights relevant examples of how SM fluorescence methodologies can illuminate the different ways in which lipids regulate the activity of membrane proteins. These studies are not limited to lipid molecules acting as ligands, but also consider how the physical properties of the bilayer can be determining factors on how membrane proteins function.Entities:
Keywords: EphA2; PIP2; SMALP; cholesterol; fluorescence resonance energy transfer; hydrophobic mismatch
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Year: 2021 PMID: 34346484 PMCID: PMC8848334 DOI: 10.1042/BST20201074
Source DB: PubMed Journal: Biochem Soc Trans ISSN: 0300-5127 Impact factor: 5.407