Description
Title: Methods for Studying Membrane Proteins in a Near-Native Membrane Environment Without the Use of Detergent
Abstract: To fully comprehend their biological function and the roles they play in the pathology of many diseases, atomic-resolution structural studies of membrane-associated proteins and peptides in a membrane environment are crucial. However, the use of common biophysical and biochemical methods has been severely constrained by the complexity of the cell membrane. Some of the key obstacles in this field have been overcome by recent developments in cryoEM and NMR spectroscopy techniques as well as the creation of novel membrane mimics. For instance, the creation of various lipid-nanodiscs has made it possible to conduct structural and functional analyses of membrane proteins as well as stable reconstitution. It has become possible to study the structure and function of membrane proteins using a variety of biophysical and biological methods thanks in particular to the ability of synthetic amphipathic polymers to isolate membrane proteins directly from the cell membrane, along with the associated membrane components like lipids, without the use of a detergent. This review article focuses on discussing the various polymers and techniques created, as well as how they are used to reconstruct membrane proteins’ functions and examine their structures. Also discussed are the special benefits and restrictions of using synthetic polymers.
Keywords: detergent-free membrane protein isolation; ionic and non-ionic polymers; lipid-nanodisc; membrane protein stability and structure; NMR; cryoEM
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Biomolecules
Writer Experience: 20+ Years
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