Nanodiscs for structural and functional studies of membrane proteins.
Membrane proteins have long presented a challenge to biochemical and functional studies. In the absence of a bilayer environment, individual proteins and critical macromolecular complexes may be insoluble and may display altered or absent activities. Nanodisc technology provides important advantages for the isolation, purification, structural resolution and functional characterization of membrane proteins. In addition, the ability to precisely control the nanodisc composition provides a nanoscale membrane surface for investigating molecular recognition events.
Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Ilia G
http://orcid.org/0000-0002-7878-2626
IG
Denisov
Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.|Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Stephen G
SG
Sligar
D000818:Animals; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D008854:Microscopy, Electron / Q000379:methods; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011487:Protein Conformation
D008051:Lipid Bilayers; D008565:Membrane Proteins