title: Nonmicellar systems for solution NMR spectroscopy of membrane proteins.
abstract: Integral membrane proteins play essential roles in many biological processes, such as energy transduction, transport of molecules, and signaling. The correct function of membrane proteins is likely to depend strongly on the chemical and physical properties of the membrane. However, membrane proteins are not accessible to many biophysical methods in their native cellular membrane. A major limitation for their functional and structural characterization is thus the requirement for an artificial environment that mimics the native membrane to preserve the integrity and stability of the membrane protein. Most commonly employed are detergent micelles, which can however be detrimental to membrane protein activity and stability. Here, we review recent developments for alternative, nonmicellar solubilization techniques, with a particular focus on their application to solution NMR studies. We discuss the use of amphipols and lipid bilayer systems, such as bicelles and nanolipoprotein particles (NLPs). The latter show great promise for structural studies in near native membranes.
authors.affiliation: Harvard Medical School, Boston, MA 02115, USA.
authors.forename: Thomas
authors.initials: T
authors.lastname: Raschle
authors.forename: Sebastian
authors.initials: S
authors.lastname: Hiller
authors.forename: Manuel
authors.initials: M
authors.lastname: Etzkorn
authors.forename: Gerhard
authors.initials: G
authors.lastname: Wagner
mesh_terms: D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry; D008074:Lipoproteins / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D012996:Solutions
chemical_list: D008051:Lipid Bilayers; D008074:Lipoproteins; D008565:Membrane Proteins; D012996:Solutions